Histone Deacetylase SIRT1 Targets Plk2 to Regulate Centriole Duplication

Histone Deacetylase SIRT1 Targets Plk2 to Regulate Centriole Duplication

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sensationnel kiyari Summary: 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.In late G1, SIRT1 is hypophosphorylated and its affinity to Plk2 is decreased, resulting in a rapid accumulation of centrosomal Plk2, which contributes to the timely initiation of centriole duplication.Collectively, our findings uncover a critical role of SIRT1 in sigma lambda gamma line jacket centriole duplication and provide a mechanistic insight into SIRT1-mediated centrosome-associated functions.

: Ling et al.demonstrate that SIRT1 deacetylates and thereby destabilizes Plk2, which in turn results in the suppression of centriole duplication.