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Science 6 June 1997:
Vol. 276. no. 5318, pp. 1571 - 1574
DOI: 10.1126/science.276.5318.1571
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Reports

Membrane and Morphological Changes in Apoptotic Cells Regulated by Caspase-Mediated Activation of PAK2

Thomas Rudel, * Gary M. Bokoch dagger

Apoptosis of Jurkat T cells induced the caspase-mediated proteolytic cleavage of p21-activated kinase 2 (PAK2). Cleavage occurred between the amino-terminal regulatory domain and the carboxyl-terminal catalytic domain, which generated a constitutively active PAK2 fragment. Stable Jurkat cell lines that expressed a dominant-negative PAK mutant were resistant to the Fas-induced formation of apoptotic bodies, but had an enhanced externalization of phosphatidylserine at the cell surface. Thus, proteolytic activation of PAK2 represents a guanosine triphosphatase-independent mechanism of PAK regulation that allows PAK2 to regulate morphological changes that are seen in apoptotic cells.

Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA
*   Present address: Max-Planck-Institut für Infektionsbiologie, Abt. Molekulare Biologie, Mobijoustrassse 2, D-10117 Berlin, Germany.

dagger    To whom correspondence should be addressed.

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J. Biol. Chem. 275, 8487-8491
   Abstract »    Full Text »    PDF »
Fas Drives Cell Cycle Progression in Glioma Cells via Extracellular Signal-regulated Kinase Activation.
H. Shinohara, H. Yagita, Y. Ikawa, and N. Oyaizu (2000)
Cancer Res. 60, 1766-1772
   Abstract »    Full Text »
Morphologic and biochemical hallmarks of apoptosis.
A. Saraste and K. Pulkki (2000)
Cardiovasc Res 45, 528-537
   Abstract »    Full Text »    PDF »
p21-Activated Kinase 1 Phosphorylates the Death Agonist Bad and Protects Cells from Apoptosis.
A. Schürmann, A. F. Mooney, L. C. Sanders, M. A. Sells, H. G. Wang, J. C. Reed, and G. M. Bokoch (2000)
Mol. Cell. Biol. 20, 453-461
   Abstract »    Full Text »
Caspase 3 Cleavage of the Ste20-Related Kinase SLK Releases and Activates an Apoptosis-Inducing Kinase Domain and an Actin-Disassembling Region.
L. A. Sabourin, P. Seale, J. Wagner, and M. A. Rudnicki (2000)
Mol. Cell. Biol. 20, 684-696
   Abstract »    Full Text »
Induction of a 55-kDa PKN Cleavage Product by Ischemia/Reperfusion Model in the Rat Retina.
K. Sumioka, Y. Shirai, N. Sakai, T. Hashimoto, C. Tanaka, M. Yamamoto, M. Takahashi, Y. Ono, and N. Saito (2000)
Invest. Ophthalmol. Vis. Sci. 41, 29-35
   Abstract »    Full Text »
Survival and Proliferation of Cells Expressing Caspase-uncleavable Poly(ADP-ribose) Polymerase in Response to Death-inducing DNA Damage by an Alkylating Agent.
S. S. Halappanavar, Y. L. Rhun, S. Mounir, L. M. Martins, J. Huot, W. C. Earnshaw, and G. M. Shah (1999)
J. Biol. Chem. 274, 37097-37104
   Abstract »    Full Text »    PDF »
Differential Ganciclovir-mediated Cell Killing by Glutamine 125 Mutants of Herpes Simplex Virus Type 1 Thymidine Kinase.
R. R. Drake, T. N. Wilbert, T. A. Hinds, and K. M. Gilbert (1999)
J. Biol. Chem. 274, 37186-37192
   Abstract »    Full Text »    PDF »
Direct Activation of the Fission Yeast PAK Shk1 by the Novel SH3 Domain Protein, Skb5.
P. Yang, R. Pimental, H. Lai, and S. Marcus (1999)
J. Biol. Chem. 274, 36052-36057
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Direct Binding and In Vivo Regulation of the Fission Yeast p21-Activated Kinase Shk1 by the SH3 Domain Protein Scd2.
E. Chang, G. Bartholomeusz, R. Pimental, J. Chen, H. Lai, L.-h. L. Wang, P. Yang, and S. Marcus (1999)
Mol. Cell. Biol. 19, 8066-8074
   Abstract »    Full Text »    PDF »
Inositol 1,4,5-Trisphosphate Receptor Type 1 Is a Substrate for Caspase-3 and Is Cleaved during Apoptosis in a Caspase-3-dependent Manner.
J. Hirota, T. Furuichi, and K. Mikoshiba (1999)
J. Biol. Chem. 274, 34433-34437
   Abstract »    Full Text »    PDF »
Identification of a Central Phosphorylation Site in p21-activated Kinase Regulating Autoinhibition and Kinase Activity.
F. T. Zenke, C. C. King, B. P. Bohl, and G. M. Bokoch (1999)
J. Biol. Chem. 274, 32565-32573
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p21-activated Protein Kinase gamma -PAK Is Activated by Ionizing Radiation and Other DNA-damaging Agents. SIMILARITIES AND DIFFERENCES TO alpha -PAK.
J. Roig and J. A. Traugh (1999)
J. Biol. Chem. 274, 31119-31122
   Abstract »    Full Text »    PDF »
The Endoplasmic Reticulum Chaperone Glycoprotein GRP94 with Ca2+-binding and Antiapoptotic Properties Is a Novel Proteolytic Target of Calpain during Etoposide-induced Apoptosis.
R. K. Reddy, J. Lu, and A. S. Lee (1999)
J. Biol. Chem. 274, 28476-28483
   Abstract »    Full Text »    PDF »
Extranuclear Apoptosis: The Role of the Cytoplasm in the Execution Phase.
J. C. Mills, N. L. Stone, and R. N. Pittman (1999)
J. Cell Biol. 146, 703-708
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