Journal
METHODS
Volume 77-78, Issue -, Pages 75-81Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2014.10.015
Keywords
PTEN; Posttranslational modification; Phosphorylation; Kinases; CK2; GSK3; PLK3; Src; C-terminal tail; C2 domain
Funding
- Fundacao para a Ciencia e a Tecnologia (FCT), Portugal [PTDC/SAU-ONC/113202/2009, PTDC/SAU-ONC/122428/2010]
- FCT Starting and Consolidator Investigator
- Fundação para a Ciência e a Tecnologia [PTDC/SAU-ONC/113202/2009, PTDC/SAU-ONC/122428/2010] Funding Source: FCT
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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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