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The polo‐like kinase Plx1 is required for M phase exit and destruction of mitotic regulators in Xenopus egg extracts
Author(s) -
Descombes Patrick,
Nigg Erich A.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.5.1328
Subject(s) - biology , polo like kinase , cytokinesis , mitosis , microbiology and biotechnology , xenopus , cyclin dependent kinase 1 , mitotic exit , cdc25 , anaphase , interphase , cell cycle , cell division , genetics , gene , cell
Polo‐like kinases (Plks), named after the Drosophila gene product polo, have been implicated in the regulation of multiple aspects of mitotic progression, including the activation of the Cdc25 phosphatase, bipolar spindle formation and cytokinesis. Genetic analyses performed in yeast and Drosophila suggest a function for Plks at late stages of mitosis, but biochemical data to support such a function in vertebrate organisms are lacking. Here we have taken advantage of Xenopus egg extracts for exploring the function of Plx1, a Xenopus Plk, during the cell cycle transition from M phase to interphase (I phase). We found that the addition of a catalytically inactive Plx1 mutant to M phase‐arrested egg extracts blocked their Ca 2+ ‐induced release into interphase. Concomitantly, the proteolytic destruction of several targets of the anaphase‐promoting complex and the inactivation of the Cdc2 protein kinase (Cdk1) were prevented. Moreover, the M to I phase transition could be abolished by immunodepletion of Plx1, but was restored upon the addition of recombinant Plx1. These results demonstrate that the exit of egg extracts from M phase arrest requires active Plx1, and they strongly suggest an important role for Plx1 in the activation of the proteolytic machinery that controls the exit from mitosis.