The G2-to-M transition from a phosphatase perspective: a new vision of the meiotic division

Cell Division
Tom LemonnierCatherine Jessus

Abstract

Cell division is orchestrated by the phosphorylation and dephosphorylation of thousands of proteins. These post-translational modifications underlie the molecular cascades converging to the activation of the universal mitotic kinase, Cdk1, and entry into cell division. They also govern the structural events that sustain the mechanics of cell division. While the role of protein kinases in mitosis has been well documented by decades of investigations, little was known regarding the control of protein phosphatases until the recent years. However, the regulation of phosphatase activities is as essential as kinases in controlling the activation of Cdk1 to enter M-phase. The regulation and the function of phosphatases result from post-translational modifications but also from the combinatorial association between conserved catalytic subunits and regulatory subunits that drive their substrate specificity, their cellular localization and their activity. It now appears that sequential dephosphorylations orchestrated by a network of phosphatase activities trigger Cdk1 activation and then order the structural events necessary for the timely execution of cell division. This review discusses a series of recent works describing the important...Continue Reading

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Citations

Jun 25, 2020·Cells·Ferdinand MeneauEnrico Maria Daldello
Mar 7, 2021·Biochemical and Biophysical Research Communications·Atsuhiro TsutiyaTomohiro Kato

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Methods Mentioned

BETA
dissection
ubiquitination

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