The acidic regions of WASp and N‐WASP can synergize with CDC42Hs and Rac1 to induce filopodia and lamellipodia

FEBS Letters

Linder, Stefan²  Aepfelbacher, Martin¹  Hüfner, Katharina²  Schell, Barbara² 

[1] Max von Pettenkofer-Institut für Medizinische Mikrobiologie, Ludwig-Maximilians-Universität, Pettenkoferstr. 9, 80336 Munich, Germany;Institut für Prophylaxe und Epidemiologie der Kreislaufkrankheiten, Ludwig-Maximilians-Universität, Pettenkoferstr. 9, 80336 Munich, Germany

关键词: Actin cytoskeleton;    WASp family protein;    Arp2/3 complex;    Filopodium;    Lamellipodium;   

DOI  :  10.1016/S0014-5793(02)02358-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The acidic (A) region of WASp family proteins is thought to represent a high-affinity binding site for Arp2/3 complex without activating properties. Here we show that GST-fused WASp-A and N-WASP-A, but not a WASP-A/W500S mutant, several truncated WASp-A constructs or WAVE1-A can pull down Arp2/3 complex from cell lysates. Significantly, WASp-A and N-WASP-A synergistically trigger formation of filopodia or lamellipodia when coinjected with sub-effective concentrations of V12CDC42Hs or V12Rac1, respectively, into macrophages. The ability of WASp family A region constructs to induce this effect is closely correlated with their ability to bind Arp2/3 complex in vitro. These results imply that (i) Arp2/3 complex is critically involved in filopodia and lamellipodia formation in macrophages and (ii) acidic regions of WASp and N-WASP are not simply binding sites for Arp2/3 complex but can prime it for RhoGTPase-triggered signals leading to actin nucleation.

【 授权许可】

Unknown