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Originally published In Press as doi:10.1074/jbc.M105599200 on October 16, 2001

J. Biol. Chem., Vol. 276, Issue 52, 49043-49052, December 28, 2001
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Phosphorylation of Pak1 by the p35/Cdk5 Kinase Affects Neuronal Morphology*

Tahira RashidDagger , Monisha BanerjeeDagger , and Margareta Nikolic§

From the Molecular and Developmental Neurobiology Medical Research Council Centre, New Hunt's House, King's College London, London, SE1 1UL, United Kingdom

The small GTPase Rac and its effectors, the Pak1 and p35/Cdk5 kinases, have been assigned important roles in regulating cytoskeletal dynamics in neurons. Our previous work revealed that the neuronal p35/Cdk5 kinase associates with Pak1 in a RacGTP-dependent manner, causing hyperphosphorylation and down-regulation of Pak1 kinase activity. We have now demonstrated direct phosphorylation of Pak1 on threonine 212 by the p35/Cdk5 kinase. In neuronal growth cones, Pak1 phosphorylated on Thr-212 localized to actin and tubulin-rich areas, suggesting a role in regulating growth cone dynamics. The expression of a non-phosphorylatable Pak1 mutant (Pak1A212) induced dramatic neurite disorganization. We also observed a strong association between p35/Cdk5 and the Pak1 C-terminal kinase domain. Overall, our data show that in neurons, membrane-associated, active Pak1 is regulated by the p35/Cdk5 kinase both by association and phosphorylation, which is essential for the proper regulation of the cytoskeleton during neurite outgrowth and remodeling.

* This work was supported by the Wellcome Trust BBSRC and GlaxoSmith Kline.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger These authors contributed equally to the work.

§ Recipient of a Wellcome Trust career development award. To whom correspondence should be sent. Tel.: 44-20-7848-6802; Fax: 44-20-7848-6816; E-mail: margareta.nikolic@kcl.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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