AI Article Synopsis
- PTEN is a key tumor suppressor frequently mutated in cancers, but its loss of expression often occurs without mutations in many tumors.
- It gets phosphorylated on specific sites by enzymes GSK3 and CK2, and blocking these phosphorylation events can be done with specific inhibitors in cell cultures.
- In studies on glioblastoma cell lines, inhibiting phosphorylation at Thr366 either by mutation or through GSK3 inhibitors resulted in a more stable PTEN protein, suggesting phosphorylation at this site destabilizes PTEN.
Article Abstract
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 Thr366 and Ser370 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 Thr366 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 Thr366 plays a role in destabilizing the PTEN protein.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2267318 | PMC |
| http://dx.doi.org/10.1042/BJ20061837 | DOI Listing |
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