Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of
nuclear and cytoplasmic proteins: Nutrient regulation of cellular metabolism and
physiology by O-GlcNAcylation
#MMPMID25336646
Hart GW
J Biol Chem
2014[Dec]; 289
(50
): 34422-3
PMID25336646
show ga
The dynamic cycling of N-acetylglucosamine (termed O-GlcNAcylation) on serine or
threonine residues of nuclear or cytoplasmic proteins serves as a nutrient
sensor, both independently and also via its interplay with other
post-translational modifications, to regulate signaling, transcription, and
cellular physiology. Emerging evidence suggests that dysregulation of this
ubiquitous post-translational modification contributes to the etiology of some
the most important human chronic diseases.
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