Premature p34 cdc2 Activation Required for Apoptosis

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Abstract
Activation of the serine-threonine kinase p34 cdc2 at an inappropriate time during the cell cycle leads to cell death that resembles apoptosis. Premature activation of p34 cdc2 was shown to be required for apoptosis induced by a lymphocyte granule protease. The kinase was rapidly activated and tyrosine dephosphorylated at the initiation of apoptosis. DNA fragmentation and nuclear collapse could be prevented by blocking p34 cdc2 activity with excess peptide substrate, or by inactivating p34 cdc2 in a temperature-sensitive mutant. Premature p34 cdc2 activation may be a general mechanism by which cells induced to undergo apoptosis initiate the disruption of the nucleus.