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Literature DB >> 34800629

O-GlcNAcylation regulation of cellular signaling in cancer.

Lorela Ciraku¹, Emily M Esquea¹, Mauricio J Reginato².

Abstract

O-GlcNAcylation is a post-translational modification occurring on serine/threonine residues of nuclear and cytoplasmic proteins, mediated by the enzymes OGT and OGA which catalyze the addition or removal of the UDP-GlcNAc moieties, respectively. Structural changes brought by this modification lead to alternations of protein stability, protein-protein interactions, and phosphorylation. Importantly, O-GlcNAcylation is a nutrient sensor by coupling nutrient sensing with cellular signaling. Elevated levels of OGT and O-GlcNAc have been reported in a variety of cancers and has been linked to regulation of multiple cancer signaling pathways. In this review, we discuss the most recent findings on the role of O-GlcNAcylation as a metabolic sensor in signaling pathways and immune response in cancer.

Entities: Chemical

Keywords: Metabolism; O-GlcNAc; OGT; Signaling; Transcription; cancer

Mesh：

Substances：

Year: 2021 PMID： 34800629 PMCID： PMC8712408 DOI： 10.1016/j.cellsig.2021.110201

Source DB: PubMed Journal: Cell Signal ISSN： 0898-6568 Impact factor: 4.315

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O-GlcNAcylation regulation of cellular signaling in cancer.

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