Histone Deacetylase SIRT1 Targets Plk2 to Regulate Centriole Duplication.

ABSTRACT: The protein deacetylase SIRT1 (Sirtuin 1) regulates many cellular processes, including cell-cycle progression, DNA damage response, and metabolism. Although the centrosome is a key regulator of cell-cycle progression and genome stability, little is known concerning SIRT1 controlled centrosome-associated events. Here we report that the centrosome protein Plk2 is acetylated and undergoes deacetylation by SIRT1. Acetylation protects Plk2 from ubiquitination, and SIRT1-mediated deacetylation promotes ubiquitin-dependent degradation of Plk2. SIRT1 controls centriole duplication by temporally modulating centrosomal Plk2 levels. AURKA phosphorylates SIRT1 and promotes the SIRT1-Plk2 interaction in mitosis. In early-mid G₁, phosphorylated SIRT1 deacetylates and promotes Plk2 degradation

SUBMITTER: Ling H 

PROVIDER: S-EPMC6814291 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature