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PROSITE documentation PDOC50831
SoHo domain profile


Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

SOHO, PS50831; SoHo domain profile  (MATRIX)


References

1AuthorsSparks A.B. Hoffman N.G. McConnell S.J. Fowlkes D.M. Kay B.K.
TitleCloning of ligand targets: systematic isolation of SH3 domain-containing proteins.
SourceNat. Biotechnol. 14:741-744(1996).
PubMed ID9630982
DOI10.1038/nbt0696-741

2AuthorsRibon V. Printen J.A. Hoffman N.G. Kay B.K. Saltiel A.R.
TitleA novel, multifuntional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes.
SourceMol. Cell. Biol. 18:872-879(1998).
PubMed ID9447983

3AuthorsKawabe H. Hata Y. Takeuchi M. Ide N. Mizoguchi A. Takai Y.
TitlenArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that interacts with synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP).
SourceJ. Biol. Chem. 274:30914-30918(1999).
PubMed ID10521485

4AuthorsKimura A. Baumann C.A. Chiang S.-H. Saltiel A.R.
TitleThe sorbin homology domain: a motif for the targeting of proteins to lipid rafts.
SourceProc. Natl. Acad. Sci. U.S.A. 98:9098-9103(2001).
PubMed ID11481476
DOI10.1073/pnas.151252898



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