| Type |
Details |
Score |
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
207
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
159
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
78
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
155
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
252
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
153
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
104
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
211
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
247
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
126
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Beesley PW |
| Year: |
2014 |
| Journal: |
J Neurochem |
| Title: |
The Neuroplastin adhesion molecules: key regulators of neuronal plasticity and synaptic function. |
| Volume: |
131 |
| Issue: |
3 |
| Pages: |
268-83 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Skjerpen CS |
| Year: |
2002 |
| Journal: |
EMBO J |
| Title: |
Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity. |
| Volume: |
21 |
| Issue: |
15 |
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4058-69 |
|
•
•
•
•
•
|
| Publication |
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Chellaiah A |
| Year: |
1999 |
| Journal: |
J Biol Chem |
| Title: |
Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity. |
| Volume: |
274 |
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49 |
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•
•
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Bae JH |
| Year: |
2009 |
| Journal: |
Cell |
| Title: |
The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. |
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138 |
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3 |
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•
•
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| First Author: |
ADHR Consortium. |
| Year: |
2000 |
| Journal: |
Nat Genet |
| Title: |
Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23. |
| Volume: |
26 |
| Issue: |
3 |
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345-8 |
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•
•
•
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| First Author: |
Hoshikawa M |
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1998 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Structure and expression of a novel fibroblast growth factor, FGF-17, preferentially expressed in the embryonic brain. |
| Volume: |
244 |
| Issue: |
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| Pages: |
187-91 |
|
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•
•
•
|
| Publication |
| First Author: |
Nakatake Y |
| Year: |
2001 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Identification of a novel fibroblast growth factor, FGF-22, preferentially expressed in the inner root sheath of the hair follicle. |
| Volume: |
1517 |
| Issue: |
3 |
| Pages: |
460-3 |
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•
•
•
•
•
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| Publication |
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Fernández IS |
| Year: |
2010 |
| Journal: |
J Biol Chem |
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Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors. |
| Volume: |
285 |
| Issue: |
15 |
| Pages: |
11714-29 |
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•
•
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| First Author: |
Mizukoshi E |
| Year: |
1999 |
| Journal: |
Biochem J |
| Title: |
Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin. |
| Volume: |
343 Pt 2 |
|
| Pages: |
461-6 |
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•
•
•
•
|
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Kolpakova E |
| Year: |
1998 |
| Journal: |
Biochem J |
| Title: |
Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor. |
| Volume: |
336 ( Pt 1) |
|
| Pages: |
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•
•
•
•
•
|
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| First Author: |
Shimoyama Y |
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1991 |
| Journal: |
Jpn J Cancer Res |
| Title: |
Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis. |
| Volume: |
82 |
| Issue: |
11 |
| Pages: |
1263-70 |
|
•
•
•
•
•
|
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Reich-Slotky R |
| Year: |
1995 |
| Journal: |
J Biol Chem |
| Title: |
Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificities. |
| Volume: |
270 |
| Issue: |
50 |
| Pages: |
29813-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shen B |
| Year: |
1998 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107. |
| Volume: |
252 |
| Issue: |
2 |
| Pages: |
524-8 |
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•
•
•
•
•
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| Publication |
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Soulet F |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Fibroblast growth factor-2 interacts with free ribosomal protein S19. |
| Volume: |
289 |
| Issue: |
2 |
| Pages: |
591-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kim HJ |
| Year: |
1998 |
| Journal: |
Development |
| Title: |
FGF-, BMP- and Shh-mediated signalling pathways in the regulation of cranial suture morphogenesis and calvarial bone development. |
| Volume: |
125 |
| Issue: |
7 |
| Pages: |
1241-51 |
|
•
•
•
•
•
|
| Publication |
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Laufer E |
| Year: |
1994 |
| Journal: |
Cell |
| Title: |
Sonic hedgehog and Fgf-4 act through a signaling cascade and feedback loop to integrate growth and patterning of the developing limb bud. |
| Volume: |
79 |
| Issue: |
6 |
| Pages: |
993-1003 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Armand AS |
| Year: |
2005 |
| Journal: |
J Cell Physiol |
| Title: |
FGF6 regulates muscle differentiation through a calcineurin-dependent pathway in regenerating soleus of adult mice. |
| Volume: |
204 |
| Issue: |
1 |
| Pages: |
297-308 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bosetti M |
| Year: |
2010 |
| Journal: |
J Cell Physiol |
| Title: |
Regulation of osteoblast and osteoclast functions by FGF-6. |
| Volume: |
225 |
| Issue: |
2 |
| Pages: |
466-71 |
|
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•
•
•
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| First Author: |
Rubin JS |
| Year: |
1989 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Purification and characterization of a newly identified growth factor specific for epithelial cells. |
| Volume: |
86 |
| Issue: |
3 |
| Pages: |
802-6 |
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•
•
•
•
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| Publication |
| First Author: |
Graeff RW |
| Year: |
1999 |
| Journal: |
Pediatr Res |
| Title: |
KGF and FGF-10 stimulate liquid secretion in human fetal lung. |
| Volume: |
46 |
| Issue: |
5 |
| Pages: |
523-9 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Park WY |
| Year: |
1998 |
| Journal: |
Dev Biol |
| Title: |
FGF-10 is a chemotactic factor for distal epithelial buds during lung development. |
| Volume: |
201 |
| Issue: |
2 |
| Pages: |
125-34 |
|
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•
•
•
•
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| Publication |
| First Author: |
Pereira CT |
| Year: |
2007 |
| Journal: |
J Surg Res |
| Title: |
Liposomal gene transfer of keratinocyte growth factor improves wound healing by altering growth factor and collagen expression. |
| Volume: |
139 |
| Issue: |
2 |
| Pages: |
222-8 |
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•
•
•
•
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| First Author: |
Ruehl M |
| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
The epithelial mitogen keratinocyte growth factor binds to collagens via the consensus sequence glycine-proline-hydroxyproline. |
| Volume: |
277 |
| Issue: |
30 |
| Pages: |
26872-8 |
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•
•
•
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| First Author: |
Mongiat M |
| Year: |
2000 |
| Journal: |
J Biol Chem |
| Title: |
The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7. |
| Volume: |
275 |
| Issue: |
10 |
| Pages: |
7095-100 |
|
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•
•
•
•
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Yan G |
| Year: |
1993 |
| Journal: |
Mol Cell Biol |
| Title: |
Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy. |
| Volume: |
13 |
| Issue: |
8 |
| Pages: |
4513-22 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Crossley PH |
| Year: |
1995 |
| Journal: |
Development |
| Title: |
The mouse Fgf8 gene encodes a family of polypeptides and is expressed in regions that direct outgrowth and patterning in the developing embryo. |
| Volume: |
121 |
| Issue: |
2 |
| Pages: |
439-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Liu SB |
| Year: |
2012 |
| Journal: |
Toxicology |
| Title: |
The role of androgen-induced growth factor (FGF8) on genital tubercle development in a hypospadiac male rat model of prenatal exposure to di-n-butyl phthalate. |
| Volume: |
293 |
| Issue: |
1-3 |
| Pages: |
53-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mattila MM |
| Year: |
2001 |
| Journal: |
Oncogene |
| Title: |
FGF-8b increases angiogenic capacity and tumor growth of androgen-regulated S115 breast cancer cells. |
| Volume: |
20 |
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22 |
| Pages: |
2791-804 |
|
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•
•
•
•
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Yoshiura K |
| Year: |
1997 |
| Journal: |
Am J Med Genet |
| Title: |
Genomic structure, sequence, and mapping of human FGF8 with no evidence for its role in craniosynostosis/limb defect syndromes. |
| Volume: |
72 |
| Issue: |
3 |
| Pages: |
354-62 |
|
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•
•
•
•
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| Publication |
| First Author: |
Tsai SJ |
| Year: |
2002 |
| Journal: |
Endocrinology |
| Title: |
Fibroblast growth factor-9 is an endometrial stromal growth factor. |
| Volume: |
143 |
| Issue: |
7 |
| Pages: |
2715-21 |
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•
•
•
•
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| First Author: |
Giri D |
| Year: |
1999 |
| Journal: |
J Cell Physiol |
| Title: |
FGF9 is an autocrine and paracrine prostatic growth factor expressed by prostatic stromal cells. |
| Volume: |
180 |
| Issue: |
1 |
| Pages: |
53-60 |
|
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•
•
•
•
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| Publication |
| First Author: |
Kim Y |
| Year: |
2006 |
| Journal: |
PLoS Biol |
| Title: |
Fgf9 and Wnt4 act as antagonistic signals to regulate mammalian sex determination. |
| Volume: |
4 |
| Issue: |
6 |
| Pages: |
e187 |
|
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•
•
•
•
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| Publication |
| First Author: |
Colvin JS |
| Year: |
2001 |
| Journal: |
Cell |
| Title: |
Male-to-female sex reversal in mice lacking fibroblast growth factor 9. |
| Volume: |
104 |
| Issue: |
6 |
| Pages: |
875-89 |
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•
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Emoto H |
| Year: |
1997 |
| Journal: |
J Biol Chem |
| Title: |
Structure and expression of human fibroblast growth factor-10. |
| Volume: |
272 |
| Issue: |
37 |
| Pages: |
23191-4 |
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•
•
•
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| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
Fibroblast growth factor-10 is a mitogen for urothelial cells. |
| Volume: |
277 |
| Issue: |
26 |
| Pages: |
23828-37 |
|
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•
•
•
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| First Author: |
Min H |
| Year: |
1998 |
| Journal: |
Genes Dev |
| Title: |
Fgf-10 is required for both limb and lung development and exhibits striking functional similarity to Drosophila branchless. |
| Volume: |
12 |
| Issue: |
20 |
| Pages: |
3156-61 |
|
•
•
•
•
•
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| First Author: |
Sekine K |
| Year: |
1999 |
| Journal: |
Nat Genet |
| Title: |
Fgf10 is essential for limb and lung formation. |
| Volume: |
21 |
| Issue: |
1 |
| Pages: |
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•
•
•
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| First Author: |
Jimenez PA |
| Year: |
1999 |
| Journal: |
J Surg Res |
| Title: |
Keratinocyte growth factor-2 accelerates wound healing in incisional wounds. |
| Volume: |
81 |
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2 |
| Pages: |
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•
•
•
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| First Author: |
Liu Y |
| Year: |
1997 |
| Journal: |
Cytogenet Cell Genet |
| Title: |
Assignment of FGF12, the human FGF homologous factor 1 gene, to chromosome 3q29-->3qter by fluorescence in situ hybridization. |
| Volume: |
78 |
| Issue: |
1 |
| Pages: |
48-9 |
|
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•
•
•
•
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| Publication |
| First Author: |
Leung KH |
| Year: |
1998 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Functional effects of FGF-13 on human lung fibroblasts, dermal microvascular endothelial cells, and aortic smooth muscle cells. |
| Volume: |
250 |
| Issue: |
1 |
| Pages: |
137-42 |
|
•
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•
•
•
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| First Author: |
Wittmack EK |
| Year: |
2004 |
| Journal: |
J Neurosci |
| Title: |
Fibroblast growth factor homologous factor 2B: association with Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root axons. |
| Volume: |
24 |
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30 |
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6765-75 |
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•
•
•
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Gecz J |
| Year: |
1999 |
| Journal: |
Hum Genet |
| Title: |
Fibroblast growth factor homologous factor 2 (FHF2): gene structure, expression and mapping to the Börjeson-Forssman-Lehmann syndrome region in Xq26 delineated by a duplication breakpoint in a BFLS-like patient. |
| Volume: |
104 |
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1 |
| Pages: |
56-63 |
|
•
•
•
•
•
|
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| First Author: |
Wang Q |
| Year: |
2000 |
| Journal: |
Mech Dev |
| Title: |
Subcellular and developmental expression of alternatively spliced forms of fibroblast growth factor 14. |
| Volume: |
90 |
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2 |
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283-7 |
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•
•
•
•
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| First Author: |
van Swieten JC |
| Year: |
2003 |
| Journal: |
Am J Hum Genet |
| Title: |
A mutation in the fibroblast growth factor 14 gene is associated with autosomal dominant cerebellar ataxia [corrected]. |
| Volume: |
72 |
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1 |
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191-9 |
|
•
•
•
•
•
|
| Publication |
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Goldfarb M |
| Year: |
2007 |
| Journal: |
Neuron |
| Title: |
Fibroblast growth factor homologous factors control neuronal excitability through modulation of voltage-gated sodium channels. |
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55 |
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3 |
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449-63 |
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•
•
•
•
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Konishi M |
| Year: |
2000 |
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J Biol Chem |
| Title: |
Fibroblast growth factor-16 is a growth factor for embryonic brown adipocytes. |
| Volume: |
275 |
| Issue: |
16 |
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•
•
•
•
|
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| Year: |
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Eur J Neurosci |
| Title: |
Identification and characterization of a novel member of the fibroblast growth factor family. |
| Volume: |
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5 |
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|
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•
•
•
•
|
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| Year: |
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Mech Dev |
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Genomic structure, mapping, activity and expression of fibroblast growth factor 17. |
| Volume: |
83 |
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1-2 |
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165-78 |
|
•
•
•
•
•
|
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| First Author: |
Kirikoshi H |
| Year: |
2000 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Molecular cloning and characterization of human FGF-20 on chromosome 8p21.3-p22. |
| Volume: |
274 |
| Issue: |
2 |
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337-43 |
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•
•
•
•
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| Year: |
2000 |
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Biochem Biophys Res Commun |
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FGF-20, a novel neurotrophic factor, preferentially expressed in the substantia nigra pars compacta of rat brain. |
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277 |
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2 |
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•
•
•
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| Year: |
2001 |
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Cancer Res |
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Identification of a novel human fibroblast growth factor and characterization of its role in oncogenesis. |
| Volume: |
61 |
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7 |
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•
•
•
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Umemori H |
| Year: |
2004 |
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Cell |
| Title: |
FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain. |
| Volume: |
118 |
| Issue: |
2 |
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•
•
•
•
|
| Publication |
| First Author: |
Quarles LD |
| Year: |
2012 |
| Journal: |
Nat Rev Endocrinol |
| Title: |
Skeletal secretion of FGF-23 regulates phosphate and vitamin D metabolism. |
| Volume: |
8 |
| Issue: |
5 |
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276-86 |
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•
•
•
•
|
| Publication |
| First Author: |
Jüppner H |
| Year: |
2011 |
| Journal: |
Kidney Int Suppl |
| Title: |
Phosphate and FGF-23. |
|
| Issue: |
121 |
| Pages: |
S24-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fukumoto S |
| Year: |
2008 |
| Journal: |
Intern Med |
| Title: |
Physiological regulation and disorders of phosphate metabolism--pivotal role of fibroblast growth factor 23. |
| Volume: |
47 |
| Issue: |
5 |
| Pages: |
337-43 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bowe AE |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate. |
| Volume: |
284 |
| Issue: |
4 |
| Pages: |
977-81 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 22 (FGF22), which plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis, and has been shown to stimulate cell proliferation in vitro [, ]. FGF22 is expressed in skin, with low expression found in brain. In mouse FGF22 is preferentially expressed in the inner root sheath of the hair follicle, which suggests a role in hair development []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 21 (FGF21), which stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression []. FGF21 has been shown to protect animals from diet-induced obesity when overexpressed in transgenic mice. It also lowers blood glucose and triglyceride levels when administered to diabetic rodents [], suggesting it may exhibit the therapeutic characteristics necessary for effective treatment of diabetes. Treatment of animals with FGF21 results in increased energy expenditure, fat utilisation and lipid excretion []. FGF21 is most abundantly expressed in the liver, and also expressed in the thymus at lower levels []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 16 (FGF16). The protein plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development []. In rat embryos, FGF16 is detected predominantly in brown adipose tissue, where it shows significant mitogenic activity for primary brown adipocytes, mediated by activation of FGFR4 []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 17 (FGF17). The protein plays an important role in the regulation of embryonic development and in the induction and patterning of the embryonic brain. It is required for normal brain development []. In mouse, FGF17 is localised to specific sites in the brain, the developing skeleton and developing arteries, which suggests a role in central nervous system, bone and vascular growth [, , ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, andirregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 14 (FGF14), also known as fibroblast growth factor homologous factor 4. In mouse, FGF14 is widely expressed in the brain, spinal cord, major arteries and thymus []. The protein is involved in neuronal development and function. FGF14-deficient mice suffer from severe ataxia and other neurological deficits []. Defects in the human FGF14 gene cause Spinocerebellar ataxia, characterised by ataxia with tremor, orofacial dyskinesia, psychiatric symptoms and cognitive deficits []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 20 (FGF20). It is involved in embryonic development, cell growth, morphogenesis, tissue repair, and tumour growth and invasion [, , ]. FGF20 is expressed in normal brain, particularly the cerebellum [], and has been shown to enhance the survival of midbrain dopaminergic neurons in vitro []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 13 (FGF13), also known as fibroblast growth factor homologous factor 2. It is thought to be involved in nervous system development and function []. FGF13 has been shown to induce cell growth of lung fibroblasts and aortic smooth muscle cells, but has no effect on dermal vascular endothelial cells []. It also is thought to regulate voltage-gated sodium channels transport and function, and play a role in MAPK signaling []. The localisation and tissue-specific expression pattern of FGF13 has made it a possible candidate for familial cases of Borjeson-Forssman-Lehmann syndrome (BFLS) and other syndromal and nonspecific forms of X-linked mental retardation []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 23 (FGF23), which is secreted by osteoblasts and osteoclasts []. FGF23 acts on kidneys, where it decreases the expression of NPT2, a sodium-phosphate cotransporter in the proximal tubule []. FGF23 is responsible for phosphate metabolism, decreasing the reabsorption and increasing excretion of phosphate []. FGF23 is involved in the pathogenesis of three hypophosphatemic disorders; oncogenic osteomalacia (OOM), X-linked hypophosphatemia (XLH) and autosomal dominant hypophosphatemic rickets (ADHR). These conditions are characterised by hypophosphatemia, decreased renal phosphate reabsorption, normal or low serum calcitriol concentrations and defective skeletal mineralisation [, , ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 1 (FGF1), also known as heparin-binding growth factor 1 and acidic fibroblast growth factor. The protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, and is therefore thought to be involved in organogenesis [, , ]. In addition to interacting with FGFR1-4, FGF1 has also been shown to interact with casein kinase II subunits [], heat shock proteins []and acidic fibroblast growth factor intracellular-binding protein []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 10 (FGF10), also known as keratinocyte growth factor 2. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7 []. Studies suggest FGF10 is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of limb bud formation [, , ]. FGF10 is also implicated as a primary factor in the process of wound healing [, ]. FGF10 interacts with FGFR1, but has a higher affinity FGFR2 [, ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 12 (FGF12), also known as fibroblast growth factor homologous factor 1. It lacks the N-terminal signal sequence present in most of the FGF family members, but it contains clusters of basic residues that have been demonstrated to act as a nuclear localisation signal. When transfected into mammalian cells, it accumulates in the nucleus, but is not secreted []. Although it currently has no known function, it is thought to be involved in nervous system development and function [, ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 9 (FGF9), also known as glia-activating factor and heparin-binding growth factor 9. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. It is involved in cyclic proliferation of uterine endometrial stroma []and can act as both a paracrine mitogen for epithelial cells and an autocrine mitogen for stromal cells []. FGF9 has also been shown to play a vital role in male development, as it is needed to carry out important masculinising developmental functions, such testicular embryogenesis [, ]. FGF9 Interacts with FGFR1, FGFR2, FGFR3 and FGFR4, but has highest affinity for FGFR3 [, ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 6 (FGF6). This protein plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration [, , ]. It may also regulate bone metabolism, as shown by its activity on both osteoblasts and osteoclasts []. FGF6 has a high affinity for FGFR1, FGFR2 and FGFR4 []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 8 (FGF8), also known as androgen-induced growth factor. It plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF8 is also required for normal brain, eye, ear and limb development during embryogenesis, and is required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system [, , , , ]. Fibroblast growth factor 8 also supports androgen and anchorage independent growth of mammary tumor cells []. FGF8 has an affinity for the all the growth factor receptors, but has the highest affinity with FGFR3 and FGFR4 [, ].This entry also includes the orthologous Fibroblast growth factor 8b from zebrafish. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 7 (FGF7), also known as keratinocyte growth factor (KGF). This protein plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. It is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes, but not in fibroblasts and endothelial cells []. Studies of mouse and rat have implicated FGF7 in morphogenesis of epithelium, wound repair, hair development and early lung organogenesis [, , , ]. FGF7 has a high affinity for FGFR2 and has also been shown to interact with various collagens []and heparan sulfate proteoglycan 2 (perlecan) []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 4 (FGF4), also known as heparin secretory transforming protein 1. This protein plays an important role in the regulation of embryonic development, cell proliferation and differentiation []. Studies on the mouse protein suggest a function in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway [, ]. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuousgrowth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 2 (FGF2), also known as heparin-binding growth factor 2 and basic fibroblast growth factor. The protein plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration and is a potent mitogen in vitro [, ]. FGF2 has a high affinity for FGFR1, FGFR2 and FGFR4, but a very low affinity with FGFR3 [, , , ]. FGF2 has also been shown to interact with casein kinase II subunit alpha []and some ribosomal proteins [, ]. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the C-terminal SH2 domain of phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma (PLC-gamma).PLC-gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLC-gamma is composed of a pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases []. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLC-gamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium []. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated site []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the N-terminal SH2 domain of phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma (PLC-gamma).PLC-gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLC-gamma is composed of a pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases []. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLC-gamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium []. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated site []. |
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| Publication |
| First Author: |
Jones MR |
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