Kinases, tails and more: Regulation of PTEN function by phosphorylation

被引：65

作者：

Fragoso, Rita ^{[1
]}

Barata, Joao T. ^{[1
]}

机构：

[1] Univ Lisbon, Fac Med, Inst Mol Med, P-1649028 Lisbon, Portugal

来源：

METHODS | 2015年 / 77-78卷

关键词：

PTEN; Posttranslational modification; Phosphorylation; Kinases; CK2; GSK3; PLK3; Src; C-terminal tail; C2; domain; TUMOR-SUPPRESSOR PTEN; PROTEIN STABILITY; PHOSPHATASE-ACTIVITY; INHIBITOR CX-4945; PI3K/AKT PATHWAY; PDZ DOMAIN; GENE; CANCER; HYPERACTIVATION; PTEN/MMAC1;

D O I：

10.1016/j.ymeth.2014.10.015

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphorylation regulates the conformation, stability, homo- and heterotypic protein interactions, localization, and activity of the tumor suppressor PTEN. From a simple picture, at the beginning of this millennium, recognizing that CK2 phosphorylated PTEN at the C-terminus and thereby impacted on PTEN stability and activity, research has led to a significantly more complex scenario today, where for instance GSK3, Plk3, ATM, ROCK or Src-family kinases are also gaining the spotlight in this evolving play. Here, we review the current knowledge on the kinases that phosphorylate PTEN, and on the impact that specific phosphorylation events have on PTEN function. (C) 2014 Elsevier Inc. All rights reserved.

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页码：75 / 81

页数：7

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