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Journal of Biochemistry Advance Access published online on January 3, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm034
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© 2006 The Japanese Biochemical Society

Effect of WAVE2 phosphorylation on activation of the Arp2/3 complex

Osamu Nakanishi1, Shiro Suetsugu1,2, Daisuke Yamazaki1 and Tadaomi Takenawa1

1Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokane-dai, Minato-ku, Tokyo 108-8639, Japan.
2PRESTO, JST, 4-1-8 Honcho, Kawaguchi City, Saitama 332-0012, Japan.

Address correspondence to T.T. E-mail: takenawa{at}ims.u-tokyo.ac.jp; Tel: +81-3-5449-5510; Fax: +81-3-5449-5417.

Received November 23, 2006; Accepted December 24, 2006


  Abstract

Members of the family of WASP-family Verprolin homologous proteins (WAVEs) activate the Arp2/3 complex to induce actin polymerization. The WAVE family comprises three proteins, namely, WAVE1, WAVE2, and WAVE3. Among them, WAVE2 is crucial for activation of the Arp2/3 complex for the formation of branched actin filaments in lamellipodia. Activation of mitogen-activated protein (MAP) kinase signaling results in the phosphorylation of the WAVE family proteins; however, which of the three WAVE proteins is phosphorylated is unclear. We found that in vitro WAVE2 is directly phosphorylated by a MAP kinase, i.e., extracellular signal-regulated kinase (ERK) 2. The proline-rich region and the verprolin, cofilin, and acidic (VCA) region of WAVE2 were phosphorylated. Interestingly, the phosphorylated VCA region had a higher affinity for the Arp2/3 complex. However, the phosphorylation of the VCA region resulted in reduced induction of Arp2/3-mediated actin polymerization in vitro. The role of the phosphorylation of the proline-rich region was not determined.

Key Words: Arp2/3 complex, lamellipodia, MAP kinase, vinculin, WAVE2


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