Premium
The acidic regions of WASp and N‐WASP can synergize with CDC42Hs and Rac1 to induce filopodia and lamellipodia
Author(s) -
Hüfner Katharina,
Schell Barbara,
Aepfelbacher Martin,
Linder Stefan
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02358-x
Subject(s) - lamellipodium , filopodia , microbiology and biotechnology , actin , rac1 , biology , pseudopodia , cytoskeleton , chemistry , biochemistry , cell , signal transduction
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.