O-GlcNAcase: Promiscuous Hexosaminidase or Key Regulator of O-GlcNAc Signaling?

被引：48
作者：
Alonso, Jana [1 ]
Schimpl, Marianne [1 ]
van Aalten, Daan M. F. [1 ,2 ]
机构：
[1] Univ Dundee, MRC, Prot Phosphorylat & Ubiquitylat Unit, Dundee DD1 5EH, Scotland
[2] Univ Dundee, Coll Life Sci, Div Mol Microbiol, Dundee DD1 5EH, Scotland
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2014年 / 289卷 / 50期
基金：
英国医学研究理事会; 英国惠康基金;
关键词：
Cell Signaling; Enzyme Inhibitor; Epigenetics; Genetics; Glycobiology; Protein Structure; BETA-N-ACETYLGLUCOSAMINIDASE; EMBRYONIC STEM-CELLS; TAY-SACHS-DISEASE; INSULIN-RESISTANCE; SUBSTRATE RECOGNITION; PROTEIN MODIFICATION; STRUCTURAL INSIGHTS; CYTOSOLIC PROTEINS; 3T3-L1; ADIPOCYTES; KINETIC-ANALYSIS;
D O I：
10.1074/jbc.R114.609198
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
O-GlcNAc signaling is regulated by an opposing pair of enzymes: O-GlcNAc transferase installs and O-GlcNAcase (OGA) removes the modification from proteins. The dynamics and regulation of this process are only beginning to be understood as the physiological functions of both enzymes are being probed using genetic and pharmacological approaches. This minireview charts the discovery and functional and structural analysis of OGA and summarizes the insights gained from recent studies using OGA inhibition, gene knock-out, and overexpression. We identify several areas of known unknowns that would benefit from future research, such as the enigmatic C-terminal domain of OGA.
引用
收藏
页码：34433 / 34439
页数：7
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