Skip to Content
Merck
  • CCDC84 Acetylation Oscillation Regulates Centrosome Duplication by Modulating HsSAS-6 Degradation.

CCDC84 Acetylation Oscillation Regulates Centrosome Duplication by Modulating HsSAS-6 Degradation.

Cell reports (2019-11-14)
Tianning Wang, Yuhong Zou, Ning Huang, Junlin Teng, Jianguo Chen
ABSTRACT

In animal cells, centriole number is strictly controlled in order to guarantee faithful cell division and genetic stability, but the mechanism by which the accuracy of centrosome duplication is maintained is not fully understood. Here, we show that CCDC84 constrains centriole number by modulating APC/CCdh1-mediated HsSAS-6 degradation. More importantly, CCDC84 acetylation oscillates throughout the cell cycle, and the acetylation state of CCDC84 at lysine 31 is regulated by the deacetylase SIRT1 and the acetyltransferase NAT10. Deacetylated CCDC84 is responsible for its centrosome targeting, and acetylated CCDC84 promotes HsSAS-6 ubiquitination by enhancing the binding affinity of HsSAS-6 for Cdh1. Our findings shed new light on the function of (de)acetylation in centriole number regulation as well as refine the established centrosome duplication model.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-γ-Tubulin antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
Sigma-Aldrich
RO-3306, ≥98% (HPLC)
Sigma-Aldrich
Nocodazole, ≥99% (TLC), powder
Sigma-Aldrich
Monoclonal ANTI-FLAG® M2 antibody produced in mouse, 1 mg/mL, clone M2, affinity isolated antibody, buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)
Sigma-Aldrich
Trichostatin A, Ready Made Solution, 5 mM in DMSO, from Streptomyces sp.
Sigma-Aldrich
(R)-MG132
Sigma-Aldrich
Anti-α-Tubulin antibody, Mouse monoclonal, clone DM1A, purified from hybridoma cell culture
Sigma-Aldrich
Hydroxyurea, 98%, powder
Sigma-Aldrich
Monoclonal Anti-HA antibody produced in mouse, clone HA-7, ascites fluid