O-GlcNAcylation: A sweet thorn in the spindle!
نویسندگان
چکیده
منابع مشابه
O-GlcNAcylation: The Sweet Side of the Cancer
O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational modification involved in a wide range of biological processes and diseases such as cancer. This modification can increase and decrease the activity of enzymes as well as interfere with protein stability and interaction. Th...
متن کاملSweet connections: O-GlcNAcylation links cancer cell metabolism and survival
Increased O-GlcNAcylation is emerging as a general characteristic of cancer cells that is critical for multiple oncogenic phenotypes. Recently, we demonstrated that elevated O-GlcNAcylation contributes to the metabolic shift seen in cancer through stabilization of the glycolytic regulator HIF-1α and links metabolism to stress and cancer cell survival.
متن کاملO-GlcNAcylation of a circadian clock protein: dPER taking its sweet time.
In this issue of Genes & Development, Kim and colleagues (pp. 490-502) report that the Drosophila circadian repressor dPER undergoes O-linked GlcNAcylation (O-GlcNAc). Their data show that manipulation of the relevant O-GlcNAc transferase (OGT) regulates behavioral rhythmicity by affecting the stability and nuclear translocation of dPER.
متن کاملO-GlcNAcylation: A New Cancer Hallmark?
O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a reversible post-translational modification consisting in the addition of a sugar moiety to serine/threonine residues of cytosolic or nuclear proteins. Catalyzed by O-GlcNAc-transferase (OGT) and removed by O-GlcNAcase, this dynamic modification is dependent on environmental glucose concentration. O-GlcNAcylation regulates the activities ...
متن کاملolecular mechanisms of O-GlcNAcylation
Protein glycosylation with O-linked N-acetylglucosamine (OGlcNAc) is a reversible post-translational modification of serines/threonines on metazoan proteins and occurring with similar time scales, dynamics and stoichiometry as protein phosphorylation. Levels of this modification are regulated by two enzymes—O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (OGA). Although the biochemistry of th...
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ژورنال
عنوان ژورنال: Cell Cycle
سال: 2016
ISSN: 1538-4101,1551-4005
DOI: 10.1080/15384101.2016.1192449