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Mol Cell Biol, April 1998, p. 2153-2163, Vol. 18, No. 4
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

A Conserved Negative Regulatory Region in alpha PAK: Inhibition of PAK Kinases Reveals Their Morphological Roles Downstream of Cdc42 and Rac1

Zhou-Shen Zhao,1 Edward Manser,1 Xiang-Qun Chen,1 Claire Chong,1 Thomas Leung,1 and Louis Lim1,2,*

Glaxo-IMCB Group, Institute of Molecular & Cell Biology, Singapore 117609, Singapore,1 and Institute of Neurology, London WC1N 1PJ, United Kingdom2

Received 17 September 1997/Returned for modification 24 November 1997/Accepted 22 December 1997

alpha PAK in a constitutively active form can exert morphological effects (E. Manser, H.-Y. Huang, T.-H. Loo, X.-Q. Chen, J.-M. Dong, T. Leung, and L. Lim, Mol. Cell. Biol. 17:1129-1143, 1997) resembling those of Cdc42G12V. PAK family kinases, conserved from yeasts to humans, are directly activated by Cdc42 or Rac1 through interaction with a conserved N-terminal motif (corresponding to residues 71 to 137 in alpha PAK). alpha PAK mutants with substitutions in this motif that resulted in severely reduced Cdc42 binding can be recruited normally to Cdc42G12V-driven focal complexes. Mutation of residues in the C-terminal portion of the motif (residues 101 to 137), though not affecting Cdc42 binding, produced a constitutively active kinase, suggesting this to be a negative regulatory region. Indeed, a 67-residue polypeptide encoding alpha PAK83-149 potently inhibited GTPgamma S-bound Cdc42-mediated kinase activation of both alpha PAK and beta PAK. Coexpression of this PAK inhibitor with Cdc42G12V prevented the formation of peripheral actin microspikes and associated loss of stress fibers normally induced by the p21. Coexpression of PAK inhibitor with Rac1G12V also prevented loss of stress fibers but not ruffling induced by the p21. Coexpression of alpha PAK83-149 completely blocked the phenotypic effects of hyperactive alpha PAKL107F in promoting dissolution of focal adhesions and actin stress fibers. These results, coupled with previous observations with constitutively active PAK, demonstrate that these kinases play an important role downstream of Cdc42 and Rac1 in cytoskeletal reorganization.

* Corresponding author. Mailing address: Glaxo-IMCB Group, Institute of Molecular & Cell Biology, 30 Medical Dr., Singapore 117609, Singapore. Phone: (65) 874-6167. Fax: (65) 774-0742. E-mail: L.Lim{at}ion.ucl.ac.uk.




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