WASP interacting proteins (WIP) family includes WIPF1 (WIP), WIPF2 (WIRE,WICH) and WIPF3 (CR16, corticosteroids and regional expression-16). WIPs share a specific proline rich sequence that interacts with the WH1 domain of WASP and N-WASP (WASL). WIPs form heterocomplexes with WASPs and may contribute to the WASP protein stability (Aspenstrom 2002, Kato et al. 2002, Ho et al. 2001, Moreau et al. 2000).
SH3 domain containing adaptor proteins like GRB2 (Carlier et al. 2000), NCK (Rohatgi et al. 2001) and WISH (DIP/SPIN90) (Fukuoka et al. 2001) bind to the proline rich domain in WASPs and activate the ARP2/3 complex. By binding simultaneously to N-WASP and the ARP2/3 complex, GRB2 works synergistically with CDC42 in the activation of ARP2/3 complex-mediated actin assembly (Carlier et al. 2000).
|10878810||A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization||Nat Cell Biol||2000|
|11157975||A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42||J Cell Biol||2001|
|11553796||CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family||Proc Natl Acad Sci U S A||2001|
|10781580||GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex||J Biol Chem||2000|
|11340081||Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway||J Biol Chem||2001|
|12213210||The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor receptor||Exp Cell Res||2002|
|11829459||WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation||Biochem Biophys Res Commun||2002|