Mechanisms regulating phosphatase specificity and the removal of individual phosphorylation sites during mitotic exit

Inside the Cell

Samuel Rogers¹  Rachael McCloy¹  D&thinspNeil Watkins¹ 

[1] The Kinghorn Cancer Center, Garvan Institute of Medical Research, Darlinghurst, NSW, Australia

关键词: Cdk1;    kinase;    mitotic exit;    phosphatase;    phosphorylation;    PP2A;    PP1;   

DOI  :  10.1002/icl3.1035

来源: Wiley

【 摘 要 】

Abstract

Entry into mitosis is driven by the activity of kinases, which phosphorylate over 7000 proteins on multiple sites. For cells to exit mitosis and segregate their genome correctly, these phosphorylations must be removed in a specific temporal order. This raises a critical and important question: how are specific phosphorylation sites on an individual protein removed? Traditionally, the temporal order of dephosphorylation was attributed to decreasing kinase activity. However, recent evidence in human cells has identified unique patterns of dephosphorylation during mammalian mitotic exit that cannot be fully explained by the loss of kinase activity. This suggests that specificity is determined in part by phosphatases. In this review, we explore how the physicochemical properties of an individual phosphosite and its surrounding amino acids can affect interactions with a phosphatase. These positive and negative interactions in turn help determine the specific pattern of dephosphorylation required for correct mitotic exit.

【 授权许可】

CC BY   
© 2015 The Authors. Inside the Cell published by WILEY Periodicals, Inc.

Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.