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
The profile we developed covers the region of the SoHo domain necessary for
the interaction with flotilin.
September 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Sparks A.B. Hoffman N.G. McConnell S.J. Fowlkes D.M. Kay B.K.
Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins.
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