Skip Navigation


Journal of Biochemistry Advance Access originally published online on January 3, 2007
Journal of Biochemistry 2007 141(3):319-325; doi:10.1093/jb/mvm034
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
141/3/319    most recent
mvm034v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Nakanishi, O.
Right arrow Articles by Takenawa, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakanishi, O.
Right arrow Articles by Takenawa, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 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; and 2PRESTO, JST, 4-1-8 Honcho, Kawaguchi City, Saitama 332-0012, Japan

*To whom correspondence should be addressed. Tel: +81-3-5449-5510, Fax: +81-3-5449-5417, E-mail: takenawa{at}ims.u-tokyo.ac.jp

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 signalling 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

Abbreviations: Arp2/3, actin-related protein 2/3; MAP kinase, mitogen-activated protein kinase; WAVE2, WASP-family Verprolin homologous protein 2; WT, wild type


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
C. M. Danson, S. M. Pocha, G. B. Bloomberg, and G. O. Cory
Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity
J. Cell Sci., December 1, 2007; 120(23): 4144 - 4154.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.