期刊
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 49, 期 4, 页码 327-342出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/10409238.2014.931338
关键词
O-GlcNAc; O-GlcNAc transferase; OGT's activity assays; OGT's catalytic mechanism; OGT's inhibitors
资金
- NIDDK intramural funds (NIH)
- National Research Foundation of Korea [2011-0027257]
Posttranslational modifications (PTM) including glycosylation, phosphorylation, acetylation, methylation and ubiquitination dynamically alter the proteome. The evolutionarily conserved enzymes O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and O-GlcNAcase are responsible for the addition and removal, respectively, of the nutrient-sensitive PTM of protein serine and threonine residues with O-GlcNAc. Indeed, the O-GlcNAc modification acts at every step in the central dogma'' of molecular biology and alters signaling pathways leading to amplified or blunted biological responses. The cellular roles of OGT and the dynamic PTM O-GlcNAc have been clarified with recently developed chemical tools including high-throughput assays, structural and mechanistic studies and potent enzyme inhibitors. These evolving chemical tools complement genetic and biochemical approaches for exposing the underlying biological information conferred by O-GlcNAc cycling.
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