Letter abstract
Nature Cell Biology 10, 849 - 857 (2008)
Published online: 30 May 2008 | doi:10.1038/ncb1745
WAVE and Arp2/3 jointly inhibit filopodium formation by entering into a complex with mDia2
Petra Beli1,2, Debora Mascheroni1,2, Dalu Xu1,2 & Metello Innocenti1
Lamellipodia/ruffles and filopodia are protruding organelles containing short and highly branched or long and unbranched actin filaments, respectively1, 2, 3. The microscopic morphology, dynamic development and protein signature of both lamellipodia/ruffles and filopodia have been investigated2, 3; however, little is known about the mechanisms by which cells coordinate the formation of these actin-based extensions. Here, we show that WAVE holds mDia2 and the Arp2/3 complex in a multimolecular complex. WAVE- and Arp2/3-dependent ruffling induced by EGF does not require mDia2. Conversely, the emission of mDia2-dependent filopodia correlates with its disengagement from WAVE. Consistently, the ability of EGF, Cdc42 and serum to induce mDia2-dependent formation of filopodia is increased in the absence of either the WAVE/Abi1/Nap1/PIR121 (WANP) or the Arp2/3 complex. Reintroduction of WAVE2 into WANP-complex knockdown cells markedly reduces filopodia formation independently of actin polymerization. Thus, WAVE and the Arp2/3 complex jointly orchestrate different types of actin-based plasma membrane protrusions by promoting ruffling and inhibiting mDia2-induced filopodia.
- Institute of Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany.
- These authors contributed equally to this work.
Correspondence to: Metello Innocenti1 e-mail: innocenti@biochem2.de
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