alexa PTEN acetylation modulates its interaction with PDZ domain.


Journal of Alzheimers Disease & Parkinsonism

Author(s): Ikenoue T, Inoki K, Zhao B, Guan KL, Ikenoue T, Inoki K, Zhao B, Guan KL

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Abstract The PTEN tumor suppressor gene is frequently inactivated in human cancer. As a major tumor suppressor, PTEN function must be tightly regulated. Both phosphorylation and membrane association have been reported to regulate PTEN activity. In addition, the COOH terminus of PTEN has a typical PDZ domain-binding motif that interacts with several PDZ domain-containing proteins. In this report, we show that PTEN is acetylated on Lys(402), which is in the COOH-terminal PDZ domain-binding motif. We show that CBP plays a major role in PTEN acetylation, whereas the SIRT1 deacetylase is mainly responsible for PTEN deacetylation. Interestingly, Lys(402) acetylation modulates PTEN interaction with PDZ domain-containing proteins, indicating a potential role of acetylation in regulating PTEN function. This article was published in Cancer Res and referenced in Journal of Alzheimers Disease & Parkinsonism

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