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Search results 101 to 111 out of 111 for Farp2

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0.017s
Type Details Score
Publication
First Author: Kuo YC
Year: 2018
Journal: Sci Rep
Title: Structural analyses of FERM domain-mediated membrane localization of FARP1.
Volume: 8
Issue: 1
Pages: 10477
Publication  
First Author: Liu Z
Year: 2013
Journal: Mol Vis
Title: A novel missense mutation in the FERM domain containing 7 (FRMD7) gene causing X-linked idiopathic congenital nystagmus in a Chinese family.
Volume: 19
Pages: 1834-40
Protein Domain
Type: Domain
Description: Proteins containing this domain include FARP1, FARP2 and FRMD7. FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases []. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons []. They are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains.FRMD7 (FERM domain-containing protein 7) and Caenorhabditis elegans CFRM3 have a FERM domain that is closely related to that in FARP1 and FARP2. Both have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain []. FRMD7 has been linked to Idiopathic congenital nystagmus , an infant-onset disease with the typical features of bilateral ocular oscillations, visual impairment, and abnormal head movement []. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites [, ].
Publication
First Author: Mlechkovich G
Year: 2014
Journal: Sci Signal
Title: Distinct cytoplasmic domains in Plexin-A4 mediate diverse responses to semaphorin 3A in developing mammalian neurons.
Volume: 7
Issue: 316
Pages: ra24
Publication
First Author: Kitano K
Year: 2006
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun
Title: Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.
Volume: 62
Issue: Pt 4
Pages: 340-5
Protein
Organism: Mus musculus/domesticus
Length: 835  
Fragment?: true
Publication
First Author: Tepass U
Year: 2009
Journal: Curr Opin Genet Dev
Title: FERM proteins in animal morphogenesis.
Volume: 19
Issue: 4
Pages: 357-67
Protein
Organism: Mus musculus/domesticus
Length: 1065  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1048  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 795  
Fragment?: false