title: PTEN acetylation modulates its interaction with PDZ domain.
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.
authors.affiliation: Life Sciences Institute, University of Michigan, Ann Arbor, USA.
authors.forename: Tsuneo
authors.initials: T
authors.lastname: Ikenoue
authors.forename: Ken
authors.initials: K
authors.lastname: Inoki
authors.forename: Bin
authors.initials: B
authors.lastname: Zhao
authors.forename: Kun-Liang
authors.initials: KL
authors.lastname: Guan