| First Author | Fukuoka M | Year | 2001 |
| Journal | J Cell Biol | Volume | 152 |
| Issue | 3 | Pages | 471-82 |
| PubMed ID | 11157975 | Mgi Jnum | J:67259 |
| Mgi Id | MGI:1930316 | Doi | 10.1083/jcb.152.3.471 |
| Citation | Fukuoka M, et al. (2001) A novel neural wiskott-aldrich syndrome protein (n-wasp) binding protein, wish, induces arp2/3 complex activation independent of cdc42. J Cell Biol 152(3):471-82 |
| abstractText | We identified a novel adaptor protein that contains a Src homology (SH)3 domain, SH3 binding proline-rich sequences, and a leucine zipper-like motif and termed this protein WASP interacting SH3 protein (WISH). WISH is expressed predominantly in neural tissues and testis. It bound Ash/Grb2 through its proline-rich regions and neural Wiskott-Aldrich syndrome protein (N-WASP) through its SH3 domain. WISH strongly enhanced N-WASP-induced Arp2/3 complex activation independent of Cdc42 in vitro, resulting in rapid actin polymerization. Furthermore, coexpression of WISH and N-WASP induced marked formation of microspikes in Cos7 cells, even in the absence of stimuli. An N-WASP mutant (H208D) that cannot bind Cdc42 still induced microspike formation when coexpressed with WISH. We also examined the contribution of WISH to a rapid actin polymerization induced by brain extract in vitro. Arp2/3 complex was essential for brain extract-induced rapid actin polymerization. Addition of WISH to extracts increased actin polymerization as Cdc42 did. However, WISH unexpectedly could activate actin polymerization even in N-WASP-depleted extracts. These findings suggest that WISH activates Arp2/3 complex through N-WASP-dependent and -independent pathways without Cdc42, resulting in the rapid actin polymerization required for microspike formation. |
