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First published online November 21, 2007
doi: 10.1242/10.1242/jcs.013714

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Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity

Department of Biochemistry, Faculty of Medical and Veterinary Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK

^* Author for correspondence (e-mail: giles.cory{at}bristol.ac.uk)

Accepted 13 September 2007

The WAVE family of proteins has long been implicated in the stimulus-dependent generation of lamellipodia at the leading edge of migrating cells, with WAVE2 in particular implicated in the formation of peripheral ruffles and chemotactic migration. However, the lack of direct visualisation of cell migration in WAVE2 mutants or knockdowns has made defining the mechanisms of WAVE2 regulation during cell migration difficult. We have characterised three MAP kinase phosphorylation sites within WAVE2 and analysed fibroblast behaviour in a scratch-wound model following introduction of transgenes encoding phospho-defective WAVE2. The cells exhibited an increase in migration speed, a decrease in the persistence of migration, and disruption of polarisation of the Golgi apparatus. All these effects could be mimicked by acute knockdown of endogenous WAVE2 expression with RNAi, indicating that phosphorylation of WAVE2 by MAP kinases regulates cell polarity during migration.

Key words: MAP kinase, WAVE2, Actin, Migration, Phosphorylation

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