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Review
. 2000 Sep 18;150(6):F117-20.
doi: 10.1083/jcb.150.6.f117.

How WASP regulates actin polymerization

S H Zigmond  1
Affiliations
Review

How WASP regulates actin polymerization

S H Zigmond. J Cell Biol. .
No abstract available

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Figures

Figure 1
Figure 1
Domain structure of WASP and N-WASP with sites of interaction between COOH- and NH2-termini, and binding by other factors. The NH2 terminus of WASP and N-WASP contain an EVH1/WH1 domain that binds the proline-rich protein, WIP (Ramesh et al. 1997). The NH2 terminus of N-WASP also binds PIP2, F-actin, and, through its IQ domain, calmodulin (Miki et al. 1996; Egile et al. 1999). The GTPase-binding domain (GBD) includes a Cdc42/Rac interactive binding (CRIB) motif and surrounding sequences. The GBD preferentially binds Cdc42 over Rac, and GTP-Cdc42 over GDP-Cdc42. In N-WASP, the basic sequence (B) binds PIP2 (Rohatgi et al. 2000). The PRD binds profilin, as well as several SH3-containing proteins, including: adaptors Nck and Grb2, tyrosine kinases, PLCγ1, and syndapin I (Brunnell et al. 1996; Finan et al. 1996; Qualmann et al. 1999). The VCA/WA (WASP homology II and acidic region) domain is the minimal fragment able to activate nucleation by the Arp2/3 complex (Machesky et al. 1999). The V motif binds monomeric actin (G-actin), whereas the CA motif binds the Arp2/3 complex (Higgs and Pollard 1999; Machesky et al. 1999).
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Comment on

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