2011
DOI: 10.1146/annurev-biochem-060608-102511
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Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Abstract: O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundant and cycles on proteins with a timescale similar to protein phosphorylation. O-GlcNAc occurs in organisms ranging from some bacteria to protozoans and metazoans, including plants and nematodes up the evolutionary t… Show more

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Cited by 1,149 publications
(1,336 citation statements)
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References 230 publications
(264 reference statements)
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“…Although the bands of some O-GlcNAc proteins appeared sensitive to treatment with 2-DG, we were surprised to see that most were unaffected, which suggests that the increase in O-GlcNAc levels after T cell activation is not simply due to increased glucose metabolism promoting OGT activity. OGT activity may also depend on its interaction partners (20,22), especially because the N terminus of OGT contains multiple tetratricopeptide repeats, which usually mediate protein-protein interactions.…”
Section: Discussionmentioning
confidence: 99%
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“…Although the bands of some O-GlcNAc proteins appeared sensitive to treatment with 2-DG, we were surprised to see that most were unaffected, which suggests that the increase in O-GlcNAc levels after T cell activation is not simply due to increased glucose metabolism promoting OGT activity. OGT activity may also depend on its interaction partners (20,22), especially because the N terminus of OGT contains multiple tetratricopeptide repeats, which usually mediate protein-protein interactions.…”
Section: Discussionmentioning
confidence: 99%
“…O-GlcNAc is the only known form of intracellular glycosylation, which involves the reversible attachment of a GlcNAc monosaccharide to serine and threonine residues (20)(21)(22). Remarkably, the opposing actions of just two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), mediate the addition and removal of O-GlcNAc from the hundreds of protein substrates identified to date, including transcription factors, epigenetic regulators, and kinases (20).…”
mentioning
confidence: 99%
“…4 I and J) is presently not known. As those Ser (Thr) residues can be enzymatically deglycosylated and potentially be phosphorylated (19), modification of these regions may play important, yet-tobe-elucidated roles in NPC function and/or assembly (20). Like the fingers, in the constricted form of the pore, these glycosylated residues would be more crowded and could enhance cohesion in the constricted state of the pore (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…Many proteins are modified by multiple PTMs. These PTMs can affect each other in what is generally termed "PTM crosstalk," which has become an intense subject of current research (2,3). Examples of crosstalk entail the priming phosphorylation on a protein substrate by a single kinase that enables other kinases to phosphorylate sites in the neighborhood.…”
mentioning
confidence: 99%