Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in...Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in cells. O-GIcNAcylation often occurs on serine （Ser） and threonine （Thr） residues of the specific substrate proteins via the addition of O-GIcNAc group by OGT. It has been known that O-GIcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GIcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GIcNAcylation as ＇protein code＇ or ＇histone code＇ may provide recognition platforms or executive instructions for subse- quent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GIcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O- GIcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GIcNAcylation with epigenetic changes in intracellular biological processes.展开更多
基金This work was supported by the National Natural Science Foundation of China （Grant No. 31571316） and the Project of Jilin Province Science and Technology Development Program （No. 20140414057GH）.
文摘Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in cells. O-GIcNAcylation often occurs on serine （Ser） and threonine （Thr） residues of the specific substrate proteins via the addition of O-GIcNAc group by OGT. It has been known that O-GIcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GIcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GIcNAcylation as ＇protein code＇ or ＇histone code＇ may provide recognition platforms or executive instructions for subse- quent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GIcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O- GIcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GIcNAcylation with epigenetic changes in intracellular biological processes.
