PROSITE documentation PDOC50831SoHo domain profile
The c-Cbl-associated protein (CAB), ArgBP2 and vinexin-α each contain three C-terminal SH3 domains (see <PDOC50002>) and an N-terminal region with similarity to the gut peptide sorbin, termed the sorbin homology (SoHo) domain [1,2,3]. Whereas the SH3 domains of these proteins can bind to different signaling or cytoskeletal molecules, the SoHo domains of CAP and vinexin has been shown to interact specifically with the lipid raft-associated protein flotilin. Thus these proteins serve as adapters that link signaling or cytoskeletal proteins to the lipid raft, a microdomain of the plasma membrane enriched in cholesterol and sphingolipids that concentrates certain signaling molecules [4].
The profile we developed covers the region of the SoHo domain necessary for the interaction with flotilin.
Last update:September 2003 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Sparks A.B. Hoffman N.G. McConnell S.J. Fowlkes D.M. Kay B.K. |
Title | Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. | |
Source | Nat. Biotechnol. 14:741-744(1996). | |
PubMed ID | 9630982 | |
DOI | 10.1038/nbt0696-741 |
2 | Authors | Ribon V. Printen J.A. Hoffman N.G. Kay B.K. Saltiel A.R. |
Title | A novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes. | |
Source | Mol. Cell. Biol. 18:872-879(1998). | |
PubMed ID | 9447983 |
3 | Authors | Kawabe H. Hata Y. Takeuchi M. Ide N. Mizoguchi A. Takai Y. |
Title | nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP). | |
Source | J. Biol. Chem. 274:30914-30918(1999). | |
PubMed ID | 10521485 |
4 | Authors | Kimura A. Baumann C.A. Chiang S.-H. Saltiel A.R. |
Title | The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 98:9098-9103(2001). | |
PubMed ID | 11481476 | |
DOI | 10.1073/pnas.151252898 |
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