| Type |
Details |
Score |
| Publication |
| First Author: |
Howard JP |
| Year: |
2002 |
| Journal: |
J Cell Biol |
| Title: |
Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. |
| Volume: |
157 |
| Issue: |
2 |
| Pages: |
315-26 |
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•
•
•
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| Publication |
| First Author: |
Gourlay CW |
| Year: |
2003 |
| Journal: |
J Cell Sci |
| Title: |
An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. |
| Volume: |
116 |
| Issue: |
Pt 12 |
| Pages: |
2551-64 |
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•
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| Publication |
| First Author: |
Engqvist-Goldstein AE |
| Year: |
1999 |
| Journal: |
J Cell Biol |
| Title: |
An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. |
| Volume: |
147 |
| Issue: |
7 |
| Pages: |
1503-18 |
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•
•
•
•
|
| Publication |
| First Author: |
Hyun TS |
| Year: |
2004 |
| Journal: |
Trends Mol Med |
| Title: |
HIP1: trafficking roles and regulation of tumorigenesis. |
| Volume: |
10 |
| Issue: |
4 |
| Pages: |
194-9 |
|
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•
•
•
•
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| Publication |
| First Author: |
Wesp A |
| Year: |
1997 |
| Journal: |
Mol Biol Cell |
| Title: |
End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. |
| Volume: |
8 |
| Issue: |
11 |
| Pages: |
2291-306 |
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•
•
•
•
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| Publication |
| First Author: |
Gervais FG |
| Year: |
2002 |
| Journal: |
Nat Cell Biol |
| Title: |
Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi. |
| Volume: |
4 |
| Issue: |
2 |
| Pages: |
95-105 |
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•
•
•
•
|
| Publication |
| First Author: |
Gottfried I |
| Year: |
2009 |
| Journal: |
Cell Mol Life Sci |
| Title: |
HIP1 exhibits an early recruitment and a late stage function in the maturation of coated pits. |
| Volume: |
66 |
| Issue: |
17 |
| Pages: |
2897-911 |
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•
•
•
•
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| Publication |
| First Author: |
Mills IG |
| Year: |
2005 |
| Journal: |
J Cell Biol |
| Title: |
Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors. |
| Volume: |
170 |
| Issue: |
2 |
| Pages: |
191-200 |
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•
•
•
•
|
| Publication |
| First Author: |
Wanker EE |
| Year: |
1997 |
| Journal: |
Hum Mol Genet |
| Title: |
HIP-I: a huntingtin interacting protein isolated by the yeast two-hybrid system. |
| Volume: |
6 |
| Issue: |
3 |
| Pages: |
487-95 |
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•
•
•
•
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| Publication |
| First Author: |
Kim JH |
| Year: |
2009 |
| Journal: |
Cell Physiol Biochem |
| Title: |
HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces BAK-dependent cell death. |
| Volume: |
23 |
| Issue: |
1-3 |
| Pages: |
43-52 |
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| Protein Domain |
| Type: |
Family |
| Description: |
Huntingtin-interacting protein 1 (HIP1) belongs to the Sla2 family. HIP1 was first identified due to its interaction with huntingtin (htt), a protein that when mutated is involved in the genetic neurodegenerative disorder Huntington's disease []. Later, HIP1 was found to play a role in trafficking and is linked to cancers []. HIP1 depends on clathrin for its membrane localisation and plays a role in pits maturation and formation of the coated vesicle []. Besides endocytosis, HIP1 is also involved in cellular processes such as tumorigenesis [], transcription regulation []and cell death [].The Sla2 family, also known as Sla2p/HIP1/HIP1R family, including Sla2p from budding yeasts [], End4 from fission yeasts [], Huntingtin-interacting protein 1 (HIP1) and HIP1-related (HIP1R) from humans and mice []. They are adaptor proteins thatlink actin to clathrin and endocytosis in the clathrin-mediated endocytosis (CME) pathway. They contain the ENTH and ANTH (E/ANTH) domain that binds both inositol phospholipids and proteins that contribute to the nucleation and formation of clathrin coats on membranes []. They also contain an I/LWEQ (talin-like) domain, which is an actin-binding domain found in proteins that serve as linkers between the actin cytoskeleton and cellular compartments []. The talin-like domains of Sla2p and HIP1R have been shown to bind F-actin (filamentous actin), however, the same level of actin binding has not been observed with HIP1 []. The central domain of the Sla2p/HIP1/HIP1R proteins contains a coiled-coil domain and several consensus sequences enabling protein-protein interactions []. Yeast Sla2p has been extensively studied: Sla2p arrives at existing endocytic patches with a ~25 seconds delay relative to clathrin and dissociates simultaneously with clathrin upon recruitment of actin-related proteins [, ]. It serves as a bridge, connecting the endocytic patch to the cortical actin cytoskeleton []. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Huntingtin-interacting protein 1-related protein (HIP1R, also known as HIP-12) belongs to the Sla2 family. HIP1R is the only known mammalian relative of huntingtin-interacting protein 1 (HIP1) []. HIP1R may have a role in actin regulation during endocytosis and is shown to promote clathrin assembly. It may also be involved in the apoptotic pathway through its interaction with a member of the Bcl-2 pro-apoptotic family [].The Sla2 family, also known as Sla2p/HIP1/HIP1R family, including Sla2p from budding yeasts [], End4 from fission yeasts [], Huntingtin-interacting protein 1 (HIP1) and HIP1-related (HIP1R) from humans and mice []. They are adaptor proteins that link actin to clathrin and endocytosis in the clathrin-mediated endocytosis (CME) pathway. They contain the ENTH and ANTH (E/ANTH) domain that binds both inositol phospholipids and proteins that contribute to the nucleation and formation of clathrin coats on membranes []. They also contain an I/LWEQ (talin-like) domain, which is an actin-binding domain found in proteins that serve as linkers between the actin cytoskeleton and cellular compartments []. The talin-like domains of Sla2p and HIP1R have been shown to bind F-actin (filamentous actin), however, the same level of actin binding has not been observed with HIP1 []. The central domain of the Sla2p/HIP1/HIP1R proteins contains a coiled-coil domain and several consensus sequences enabling protein-protein interactions []. Yeast Sla2p has been extensively studied: Sla2p arrives at existing endocytic patches with a ~25 seconds delay relative to clathrin and dissociates simultaneously with clathrin upon recruitment of actin-related proteins [, ]. It serves as a bridge, connecting the endocytic patch to the cortical actin cytoskeleton []. |
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