Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit

Roberta Visconti, Luca Palazzo, Rosa Della Monica and Domenico Grieco ()
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Roberta Visconti: CEINGE Biotecnologie Avanzate
Luca Palazzo: CEINGE Biotecnologie Avanzate
Rosa Della Monica: CEINGE Biotecnologie Avanzate
Domenico Grieco: CEINGE Biotecnologie Avanzate

Nature Communications, 2012, vol. 3, issue 1, 1-11

Abstract: Abstract Correct execution of mitosis in eukaryotes relies on timely activation and inactivation of cyclin B-dependent kinase 1 (cdk1), the M-phase-promoting factor (MPF). Once activated, MPF is sustained until mitotic spindle assembly by phosphorylation-dependent feedback loops that prevent inhibitory phosphorylation of cdk1 and ubiquitin-dependent degradation of cyclin B. Whether subsequent MPF inactivation and anaphase onset require a specific phosphatase(s) to reverse these feedback loops is not known. Here we show through biochemical and genetic evidence that timely MPF inactivation requires activity of the essential RNA polymerase II-carboxy-terminal domain phosphatase Fcp1, in a transcription-independent manner. We identify Cdc20, a coactivator of the ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) required for cyclin degradation and anaphase onset, USP44, a deubiquitinating peptidase that opposes APC/C action, and Wee1, a cdk1 inhibitory kinase, as relevant Fcp1 targets. We propose that Fcp1 has a crucial role in the liaison between dephosphorylation and ubiquitination that drives mitosis exit.

Date: 2012
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1886

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DOI: 10.1038/ncomms1886

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