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. 1995 Nov 1;14(21):5297–5305. doi: 10.1002/j.1460-2075.1995.tb00214.x

Rac GTPase interacts with GAPs and target proteins through multiple effector sites.

D Diekmann 1, C D Nobes 1, P D Burbelo 1, A Abo 1, A Hall 1
PMCID: PMC394639  PMID: 7489719

Abstract

Rac, a small GTPase in the ras superfamily, regulates at least two biological processes in animal cells: (i) the polymerization of actin and the assembly of integrin complexes to produce lamellipodia and ruffles; and (ii) the activity of an NADPH oxidase in phagocytic cells. NADPH oxidase activation is mediated through a rac effector protein, p67phox, and using chimeras made between rac and the closely related GTPase, rho, we have identified two distinct effector sites in rac, one N-terminal and one C-terminal, both of which are required for activation of p67phox. The same two effector sites are essential for rac-induced actin polymerization in fibroblasts. p65PAK, a ubiquitous serine/threonine kinase, interacts with rac at both the N- and C-terminal effector sites, but the GTPase-activating protein, bcr interacts with rac at a different region. This makes p65PAK, but not bcr, a candidate effector of rac-induced lamellipodium formation.

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