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Molecular and Cellular Biology, January 2000, p. 453-461, Vol. 20, No. 2
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

p21-Activated Kinase 1 Phosphorylates the Death Agonist Bad and Protects Cells from Apoptosisdagger

A. Schürmann,1,2 A. F. Mooney,2 L. C. Sanders,2 M. A. Sells,3 H. G. Wang,4 J. C. Reed,5 and G. M. Bokoch2,*

Institut für Pharmakologie und Toxikologie, Medizinische Fakulät, Rheinisch-Westfälische Technische Hochschule Aachen, D52057 Aachen, Germany1; Departments of Immunology and Cell Biology, The Scripps Research Institute,2 and The Burnham Institute,5 La Jolla, California 92037; Fox Chase Cancer Center, Philadelphia, Pennsylvania 191113; and H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 336124

Received 19 March 1999/Returned for modification 26 April 1999/Accepted 17 October 1999

Bad is a critical regulatory component of the intrinsic cell death machinery that exerts its death-promoting effect upon heterodimerization with the antiapoptotic proteins Bcl-2 and Bcl-xL. Growth factors promote cell survival through phosphorylation of Bad, resulting in its dissociation from Bcl-2 and Bcl-xL and its association with 14-3-3tau . Survival of interleukin 3 (IL-3)-dependent FL5.12 lymphoid progenitor cells is attenuated upon treatment with the Rho GTPase-inactivating toxin B from Clostridium difficile. p21-activated kinase 1 (PAK1) is activated by IL-3 in FL5.12 cells, and this activation is reduced by the phosphatidylinositol 3-kinase inhibitor LY294002. Overexpression of a constitutively active PAK mutant (PAK1-T423E) promoted cell survival of FL5.12 and NIH 3T3 cells, while overexpression of the autoinhibitory domain of PAK (amino acids 83 to 149) enhanced apoptosis. PAK phosphorylates Bad in vitro and in vivo on Ser112 and Ser136, resulting in a markedly reduced interaction between Bad and Bcl-2 or Bcl-xL and the increased association of Bad with 14-3-3tau . Our findings indicate that PAK inhibits the proapoptotic effects of Bad by direct phosphorylation and that PAK may play an important role in cell survival pathways.

* Corresponding author. Mailing address: Departments of Immunology and Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037. Phone: (858) 784-8217. Fax: (858) 784-8218. E-mail: bokoch{at}scripps.edu.

dagger Manuscript no. 12215-IMM of The Scripps Research Institute.

Molecular and Cellular Biology, January 2000, p. 453-461, Vol. 20, No. 2
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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