Caspase-dependent activation of cyclin-dependent kinases during Fas-induced apoptosis in Jurkat cells

Bin Bing Zhou, Honglin Li, Junying Yuan, Marc W. Kirschner

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Abstract

The activation of cyclin-dependent kinases (cdks) has been implicated in apoptosis induced by various stimuli. We find that the Fas-induced activation of cdc2 and cdk2 in Jurkat cells is not dependent on protein synthesis, which is shut down very early during apoptosis before caspase-3 activation. Instead, activation of these kinases seems to result from both a rapid cleavage of Wee1 (an inhibitory kinase of cdc2 and cdk2) and inactivation of anaphase-promoting complex (the specific system for cyclin degradation), in which CDC27 homolog is cleaved during apoptosis. Both Wee1 and CDC27 are shown to be substrates of the caspase-3-like protease. Although cdk activities are elevated during Fas-induced apoptosis in Jurkat cells, general activation of the mitotic processes does not occur. Our results do not support the idea that apoptosis is simply an aberrant mitosis but, instead, suggest that a subset of mitotic mechanisms plays an important role in apoptosis through elevated cdk activities.

Original languageEnglish (US)
Pages (from-to)6785-6790
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number12
DOIs
StatePublished - Jun 9 1998

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Jurkat Cells
Cyclin-Dependent Kinases
Caspases
Apoptosis
Caspase 3
Phosphotransferases
Anaphase-Promoting Complex-Cyclosome
Cyclins
Mitosis
Peptide Hydrolases
Proteins

ASJC Scopus subject areas

  • General

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Caspase-dependent activation of cyclin-dependent kinases during Fas-induced apoptosis in Jurkat cells. / Zhou, Bin Bing; Li, Honglin; Yuan, Junying; Kirschner, Marc W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, No. 12, 09.06.1998, p. 6785-6790.

Research output: Contribution to journalArticle

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