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- W164105195 abstract "O-GlcNAcylation on serine and threosine side chains is dynamically regulated in response to various biological stimuli. O-GlcNAcyaltion shares remarkably similar features as O-phosphorylation. Dynamic regulation of O-GlcNAcylation has been found essential in many signaling events. Here, we report the perturbations of O-GlcNAcylation in response to lithium inhibition of glycogen synthase kinase-3 (GSK3), a pivotal kinase involved in many signaling pathways. By using SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 known and potential O-GlcNAcylated proteins. Quantitative measurements indicated that 12 proteins had significantly increased O-GlcNAcylation upon GSK3 inhibition, while 24 proteins showed decreases. Based on the MS data, we further investigated the potential roles of O-GlcNAc on host cell factor (HCF-1) and showed dynamic regulation of O-GlcNAcylation on HCF-1 influenced its subcellular distribution. Taken together, these data suggested roles of O-GlcNAcylation in GSK3 signaling pathways, and also validated a valuable method to globally monitor O-GlcNAc perturbations in response to biological stimuli. Supported by NIH contract N01-HV-28180. Dr. Hart receives a share of royalty received by the university on sales of the CTD 110.6 antibody. Terms of this arrangement are managed by JHU" @default.
- W164105195 created "2016-06-24" @default.
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- W164105195 date "2007-01-01" @default.
- W164105195 modified "2023-09-25" @default.
- W164105195 title "Glycogen Synthase Kinase‐3 (GSK3) Inhibition By Lithium Induces O‐GlcNAcylation Perturbations" @default.
- W164105195 doi "https://doi.org/10.1096/fasebj.21.6.a1021-a" @default.
- W164105195 hasPublicationYear "2007" @default.
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