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Title: SUMOylation of G9a regulates its function as an activator of myoblast proliferation
Authors: Srinivasan, S
Shankar, SR 
Wang, Y 
Taneja, R 
Issue Date: 1-Mar-2019
Publisher: Springer Nature
Citation: Srinivasan, S, Shankar, SR, Wang, Y, Taneja, R (2019-03-01). SUMOylation of G9a regulates its function as an activator of myoblast proliferation. Cell Death and Disease 10 (3) : 250-. ScholarBank@NUS Repository.
Abstract: © 2019, The Author(s). The lysine methyltransferase G9a plays a role in many cellular processes. It is a potent repressor of gene expression, a function attributed to its ability to methylate histone and non-histone proteins. Paradoxically, in some instances, G9a can activate gene expression. However, regulators of G9a expression and activity are poorly understood. In this study, we report that endogenous G9a is SUMOylated in proliferating skeletal myoblasts. There are four potential SUMOylation consensus motifs in G9a. Mutation of all four acceptor lysine residues [K79, K152, K256, and K799] inhibits SUMOylation. Interestingly, SUMOylation does not impact G9a-mediated repression of MyoD transcriptional activity or myogenic differentiation. In contrast, SUMO-defective G9a is unable to enhance proliferation of myoblasts. Using complementation experiments, we show that the proliferation defect of primary myoblasts from conditional G9a-deficient mice is rescued by re-expression of wild-type, but not SUMOylation-defective, G9a. Mechanistically, SUMOylation acts as signal for PCAF (P300/CBP-associated factor) recruitment at E2F1-target genes. This results in increased histone H3 lysine 9 acetylation marks at E2F1-target gene promoters that are required for S-phase progression. Our studies provide evidence by which SUMO modification of G9a influences the chromatin environment to impact cell cycle progression.
Source Title: Cell Death and Disease
ISSN: 20414889
DOI: 10.1038/s41419-019-1465-9
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