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

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Science  06 Jun 1997:
Vol. 276, Issue 5318, pp. 1571-1574
DOI: 10.1126/science.276.5318.1571

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Abstract

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.

  • * Present address: Max-Planck-Institut für Infektionsbiologie, Abt. Molekulare Biologie, Mobijoustrassse 2, D-10117 Berlin, Germany.

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