%0 Journal Article %T Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance. %+ Department of Biochemistry and Molecular Biology %+ Program in Genes and Development %+ Center for Cancer Epigenetics %+ Department of Genetics %+ Institut de génétique et biologie moléculaire et cellulaire (IGBMC) %+ Department of Hematopathology %A Atanassov, Boyko, S. %A Evrard, Yvonne, A. %A Multani, Asha, S. %A Zhang, Zhijing %A Tora, László %A Devys, Didier %A Chang, Sandy %A Dent, Sharon, Y. R. %< avec comité de lecture %@ 1097-2765 %J Molecular Cell %I Cell Press %V 35 %N 3 %P 352-64 %8 2009-08-14 %D 2009 %R 10.1016/j.molcel.2009.06.015 %M 19683498Journal articles %X Histone acetyltransferases (HATs) play important roles in gene regulation and DNA repair by influencing the accessibility of chromatin to transcription factors and repair proteins. Here, we show that deletion of Gcn5 leads to telomere dysfunction in mouse and human cells. Biochemical studies reveal that depletion of Gcn5 or ubiquitin-specific protease 22 (Usp22), which is another bona fide component of the Gcn5-containing SAGA complex, increases ubiquitination and turnover of TRF1, a primary component of the telomeric shelterin complex. Inhibition of the proteasome or overexpression of USP22 opposes this effect. The USP22 deubiquitinating module requires association with SAGA complexes for activity, and we find that depletion of Gcn5 compromises this association in mammalian cells. Thus, our results indicate that Gcn5 regulates TRF1 levels through effects on Usp22 activity and SAGA integrity. %G English %L inserm-00420788 %U https://inserm.hal.science/inserm-00420788 %~ INSERM %~ CNRS %~ UNIV-STRASBG1 %~ IGBMC %~ UNIV-STRASBG %~ SITE-ALSACE