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• W2902852662 endingPage "2865.e3" @default.
• W2902852662 startingPage "2851" @default.
• W2902852662 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. 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 centriole duplication and provide a mechanistic insight into SIRT1-mediated centrosome-associated functions." @default.
• W2902852662 created "2018-12-11" @default.
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• W2902852662 date "2018-12-01" @default.
• W2902852662 modified "2023-10-16" @default.
• W2902852662 title "Histone Deacetylase SIRT1 Targets Plk2 to Regulate Centriole Duplication" @default.
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• W2902852662 doi "https://doi.org/10.1016/j.celrep.2018.11.025" @default.
• W2902852662 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6814291" @default.
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• W2902852662 hasPublicationYear "2018" @default.
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