Mechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-Bisphosphate

doi:10.1083/jcb.150.6.1299

Published online 18 September 2000. doi:10.1083/jcb.150.6.1299

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© The Rockefeller University Press, 0021-9525/2000//1299 $5.00
The Journal of Cell Biology, Volume 150, Number 6, , 2000 1299-1310

Original Article

Mechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-Bisphosphate

Rajat Rohatgi^a, Hsin-yi Henry Ho^a, and Marc W. Kirschner^a

^a Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115.(617) 432-0420(617) 432-2250

Neuronal Wiskott-Aldrich Syndrome protein (N-WASP) transmitssignals from Cdc42 to the nucleation of actin filaments by Arp2/3complex. Although full-length N-WASP is a weak activator ofArp2/3 complex, its activity can be enhanced by upstream regulatorssuch as Cdc42 and PI(4,5)P₂. We dissected this activation reactionand found that the previously described physical interactionbetween the NH₂-terminal domain and the COOH-terminal effectordomain of N-WASP is a regulatory interaction because it caninhibit the actin nucleation activity of the effector domainby occluding the Arp2/3 binding site. This interaction betweenthe NH₂- and COOH termini must be intramolecular because insolution N-WASP is a monomer. Phosphatidylinositol 4,5-bisphosphate(PI(4,5)P₂) influences the activity of N-WASP through a conservedbasic sequence element located near the Cdc42 binding site ratherthan through the WASp homology domain 1. Like Cdc42, PI(4,5)P₂reduces the affinity between the NH₂- and COOH termini of themolecule. The use of a mutant N-WASP molecule lacking this basicstretch allowed us to delineate a signaling pathway in Xenopusextracts leading from PI(4,5)P₂ to actin nucleation throughCdc42, N-WASP, and Arp2/3 complex. In this pathway, PI(4,5)P₂serves two functions: first, as an activator of N-WASP; andsecond, as an indirect activator of Cdc42.

Key Words: phosphoinositides • Cdc42 GTP-binding protein • actin • signal transduction • Wiskott-Aldrich Syndrome protein

R. Rohatgi and H.H. Ho contributed equally to this study.

Abbreviations used in this paper: A, acidic region; BR, basicregion; C, cofilin homology segment; CRIB, Cdc42/Rac interactivemotif; G-actin, actin monomers; GBD, G-protein binding domain;G-protein, GTP binding protein; GBR, G-protein binding region;GST, glutathione S-transferase; HT, hexahistidine-tagged; HSS,high speed supernatant; MT, Myc-tagged; NMR, nuclear magneticresonance; N-WASP, neuronal WASP; PC, phosphatidylcholine; PI,phosphatidylinositol; PI(4,5)P₂, PI 4,5-bisphosphate; PRD, proline-richdomain; V, verprolin homology segment; VCA, COOH-terminal domainof WASP family proteins containing the V, C, and A segments;WASp, Wiskott-Aldrich Syndrome protein; WH1, WASp homology domain1; WIP, WASp interacting protein.

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Haugh, J. M., Meyer, T. (2002). Active EGF receptors have limited access to PtdIns(4,5)P2 in endosomes: implications for phospholipase C and PI 3-kinase signaling. J. Cell Sci. 115: 303-310 [Abstract] [Full Text]