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Significance Glycosylation is considered to be a major posttranslational modification, andO -GlcNAcylation is known to affect protein folding and function. In this study, we show that the methyltransferase EZH2, which catalyzes the methylation of histone 3 at lysine 27 to form H3K27m3, requiresO -GlcNAcylation to enhance its stability and enzymatic activity to promote tumor progression. We further show that theO -GlcNAcylation in the N-terminal region of EZH2 stabilizes the enzyme and theO -GlcNAcylation at S729 in the catalytic domain is essential for its activity of di- and trimethylation. This study indicates that selective inhibition of EZH2O -GlcNAcylation may suppress the methylation of H3K27 and thus inhibit tumor progression.

O -GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2