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J. Cell Biol. 155 (6): 1029-1042

Copyright © 2001 by the Rockefeller University Press.


A novel p21-activated kinase binds the actin and microtubule networks and induces microtubule stabilization

Julien Cau1, Sandrine Faure1, Michel Comps2, Claude Delsert2, and Nathalie Morin1

1 Centre de Recherche de Biochimie Macromoleculaire, Centre National de la Recherche Scientifique UPR 1086, 34293 Montpellier cedex 5, France
2 French Research Institute for Exploitation of the Sea (IFREMER), 17390 La Tremblade, France

Address correspondence to Nathalie Morin, Centre de Recherche de Biochimie Macromoleculaire, CNRS UPR 1086, 1919 Route de Mende, 34293 Montpellier cedex 5, France. Tel.: 33-4-6761-3330. Fax: 33-4-6752-1559. E-mail: morin{at}

Abstract: Coordination of the different cytoskeleton networks in the cell is of central importance for morphogenesis, organelle transport, and motility. The Rho family proteins are well characterized for their effects on the actin cytoskeleton, but increasing evidence indicates that they may also control microtubule (MT) dynamics. Here, we demonstrate that a novel Cdc42/Rac effector, X-p21-activated kinase (PAK)5, colocalizes and binds to both the actin and MT networks and that its subcellular localization is regulated during cell cycle progression. In transfected cells, X-PAK5 promotes the formation of stabilized MTs that are associated in bundles and interferes with MTs dynamics, slowing both the elongation and shrinkage rates and inducing long paused periods. X-PAK5 subcellular localization is regulated tightly, since coexpression with active Rac or Cdc42 induces its shuttling to actin-rich structures. Thus, X-PAK5 is a novel MT-associated protein that may communicate between the actin and MT networks during cellular responses to environmental conditions.

Key Words: PAK; actin; microtubules; stabilization; dynamics

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