Spatiotemporal regulation of the Pak1 kinase

Pak1 (p21-activated kinase 1) is a key regulator of the actin cytoskeleton, adhesion and cell motility. Such biological roles require a tight spatial and kinetic control of its localization and activity. We summarize here the current knowledge on Pak1 dynamics in vivo. Inactive dimeric Pak1 is mainl...

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Bibliographic Details
Published in:	Biochemical Society transactions Vol. 33; no. Pt 4; p. 646
Main Authors:	Parrini, M C, Matsuda, M, de Gunzburg, J
Format:	Journal Article
Language:	English
Published:	England 01-08-2005
Subjects:	Animals Catalytic Domain Cell Movement Dimerization p21-Activated Kinases Protein Conformation Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism
Online Access:	Get more information
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Summary:	Pak1 (p21-activated kinase 1) is a key regulator of the actin cytoskeleton, adhesion and cell motility. Such biological roles require a tight spatial and kinetic control of its localization and activity. We summarize here the current knowledge on Pak1 dynamics in vivo. Inactive dimeric Pak1 is mainly cytosolic. Localized interaction with the activators Cdc42-GTP and Rac1-GTP stimulates the kinase at the sites of cellular protrusions. Moreover, Pak1 is dynamically engaged into multiprotein complexes forming adhesions to the extracellular matrix. Cutting edge microscopy technologies on living cells are finally shedding light on the intricate spatiotemporal mechanisms regulating Pak1.
ISSN:	0300-5127
DOI:	10.1042/BST0330646