期刊
BIOCHEMICAL JOURNAL
卷 405, 期 -, 页码 439-444出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20061837
关键词
phosphatase; phosphoinositide; protein stability; PTEN (phosphatase and tensin homologue deleted on chromosome 10); tumour suppressor
资金
- MRC [G9403619] Funding Source: UKRI
- Medical Research Council [G9403619] Funding Source: researchfish
- Medical Research Council [G9403619] Funding Source: Medline
Although PTEN (phosphatase and tensin homologue deleted on chromosome 10) is one of the most commonly mutated tumour suppressors in human cancers, loss of PTEN expression in the absence of mutation appears to occur in an even greater number of tumours. PTEN is phosphorylated in vitro on Thr(366) and Ser(370) by GSK3 (glycogen synthase kinase 3) and CK2 (casein kinase 2) respectively, and specific inhibitors of these kinases block these phosphorylation events in cultured cells. Although mutation of these phosphorylation sites did not alter the phosphatase activity of PTEN in vitro or in cells, blocking phosphorylation of Thr(366) by either mutation or GSK3 inhibition in glioblastoma cell lines led to a stabilization of the PTEN protein. Our data support a model in which the phosphorylation of Thr(366) plays a role in destabilizing the PTEN protein.
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