PTEN: a novel anti-oncogenic function independent of phosphatase activity.
The PTEN gene is an important tumor suppressor mutated in a number of cancers. To date, its growth regulatory properties have been intimately linked to its ability to act as a protein and phosphoinositol phosphatase. Inactivation of the enzymatic activity of PTEN is primarily due to direct mutation of its amino-terminal catalytic domain but approximately 20% of mutations are in the carboxy-terminus, which regulates membrane localization, protein stability, cellular migration and p53 function. We identified a novel protein that interacts with this domain, the v-jun transcriptional target, MSP58. Binding of MSP58 to PTEN results in the suppression of MSP58-mediated transformation. However, this PTEN effect does not require its catalytic activity, suggesting additional mechanisms of PTEN action.[1]References
- PTEN: a novel anti-oncogenic function independent of phosphatase activity. Okumura, K., Zhao, M., DePinho, R.A., Furnari, F.B., Cavenee, W.K. Cell Cycle (2005) [Pubmed]
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