The PTEN protein: cellular localization and post-translational regulation. (9th February 2016)

• Record Type: Journal Article
• Authors: Leslie, Nick R.; Kriplani, Nisha; Hermida, Miguel A.; Alvarez-Garcia, Virginia; Wise, Helen M.
• Is Part Of: Biochemical Society transactions. Volume 44:Number 1(2016)
• Page Start: 273
• Page End: 278
• Publication Date: 2016-02-09
• Subjects: AKT -- cancer -- phosphatase -- phosphoinositide 3-kinase -- signal transduction -- ubiquitin; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20150224
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The phosphatase and tensin homologue deleted on chromosome 10 (PTEN) phosphatase dephosphorylates PIP3, the lipid product of the class I PI 3-kinases, and suppresses the growth and proliferation of many cell types. It has been heavily studied, in large part due to its status as a tumour suppressor, the loss of function of which is observed through diverse mechanisms in many tumour types. Here we present a concise review of our understanding of the PTEN protein and highlight recent advances, particularly in our understanding of its localization and regulation by ubiquitination and SUMOylation.