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ISSN: 2168-9431

Single Cell Biology
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Commentary

Protein Phosphatases Triggering the Dephosphorylation and Inactivation of Greatwall

Anna Castro* and Thierry Lorca*

Equipe Labellisée Ligue Contre le Cancer, Université de Montpellier, Centre de Recherche de Biologie Cellulaire de Montpellier, CNRS UMR 5237, 1919 Route de Mende, 34293, Montpellier cedex 5, France

*Corresponding Author:
Anna Castro
Equipe Labellisée Ligue Contre le Cancer
Université de Montpellier, Centre de Recherche de Biologie Cellulaire de Montpellier
CNRS UMR 5237, 1919 Route de Mende
34293, Montpellier cedex 5, France
Tel: 33434359556
Fax: 33434359410
E-mail: [email protected]
Thierry Lorca
Equipe Labellisée Ligue Contre le Cancer
Université de Montpellier, Centre de Recherche de Biologie Cellulaire de Montpellier
CNRS UMR 5237, 1919 Route de Mende
34293, Montpellier cedex 5, France
Tel: 33434359556
Fax: 33434359410
E-mail: [email protected]

Received Date: May 16, 2016; Accepted Date: June 06, 2016; Published Date: Jun 08, 2016

Citation: Castro A, Lorca T (2016) Protein Phosphatases Triggering the Dephosphorylation and Inactivation of Greatwall. Single Cell Biol 5:141. doi: 10.4172/2168-9431.1000141.

Copyright: © 2016 Castro A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Entry into mitosis requires the coordinated activation of protein kinases and phosphatases that regulate key cell cycle components allowing entry, progression and exit of mitosis. The limiting step is thought to be the activation of both Cdk1-Cyclin B and Greatwall kinases. The former promoting phosphorylation of mitotic substrates when cells enter into mitosis and the latter inhibiting PP2A-B55, responsible for dephosphorylation of these substrates. Here, we summarize recent data on the regulation of Greatwall activity and reversal of mitotic substrates phosphorylation required for mitotic exit.

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