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Journal Article
Phosphatases: providing safe passage through mitotic exit
2011
Overview
Key Points
Mitotic exit comprises all the mitotic stages after 'satisfaction' of the spindle assembly checkpoint, including chromosome segregation, cytokinesis and reassembly of interphase cell structures.
Mitotic exit is largely driven by inactivation of mitotic kinases, as well as by activation of counteracting mitotic exit phosphatases, which leads to a net dephosphorylation of a large range of substrates.
The key mitotic exit phosphatase in budding yeast is Cdc14, which is regulated by two regulatory networks: Cdc14 early anaphase release (FEAR) and mitotic exit network (MEN).
Animal cell mitotic exit depends on protein phosphatases PP1 and PP2A, and the key function of Cdc14 does not seem to be conserved in species other than budding yeast.
A regulatory network involving Greatwall kinase and its substrates, the PP2A-inhibitors α-endosulphine (ENSA) and cyclic AMP-regulated phosphoprotein 19 (ARPP19), establishes a mutual inhibition between cyclin-dependent kinase 1 (CDK1) and PP2A.
Mitotic exit phosphatases are attractive candidate targets for the development of future cancer therapeutics.
The regulation of mitotic exit requires the rapid reversal of mitotic phosphorylation on a broad range of substrates. This requires not only inactivation of mitotic kinases but also activation of protein phosphatases, which work in regulatory networks to ensure that an interphase cell is correctly established.
The mitosis-to-interphase transition involves dramatic cellular reorganization from a state that supports chromosome segregation to a state that complies with all functions of an interphase cell. This process, termed mitotic exit, depends on the removal of mitotic phosphorylations from a broad range of substrates. Mitotic exit regulation involves inactivation of mitotic kinases and activation of counteracting protein phosphatases. The key mitotic exit phosphatase in budding yeast, Cdc14, is now well understood. By contrast, in animal cells, it is now emerging that mitotic exit relies on distinct regulatory networks, including the protein phosphatases PP1 and PP2A.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 81
/ 86
/ Anaphase-Promoting Complex-Cyclosome
/ Animals
/ Biomedical and Life Sciences
/ CDC2 Protein Kinase - physiology
/ Cell Cycle Proteins - physiology
/ Enzymes
/ Humans
/ Kinases
/ Mitosis
/ Phosphoric Monoester Hydrolases - physiology
/ Protein Phosphatase 1 - physiology
/ Protein Phosphatase 2 - physiology
/ Protein Serine-Threonine Kinases - physiology
/ Protein Tyrosine Phosphatases - physiology
/ Proteins
/ Proto-Oncogene Proteins - physiology
/ Saccharomyces cerevisiae - cytology
/ Saccharomyces cerevisiae - physiology
/ Saccharomyces cerevisiae Proteins - physiology
/ Ubiquitin-Protein Ligase Complexes - physiology
/ Yeasts
