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O-GlcNAcylation regulation of cellular signaling in cancer
Journal article   Open access   Peer reviewed

O-GlcNAcylation regulation of cellular signaling in cancer

Lorela Ciraku, Emily M. Esquea and Mauricio J. Reginato
Cellular signalling, v 90, 110201
Feb 2022
PMID: 34800629
url
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8712408View
Accepted (AM)Open Access (License Unspecified) Open

Abstract

cancer Metabolism O-GlcNAc OGT Signaling Transcription
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. •The post-translational modification O-GlcNAcylation is found to be elevated in nearly all cancers.•This nutrient sensitive intracellular glycosylation can regulate a diverse set of cytosolic and nuclear proteins.•O-GlcNAcylation regulates signaling pathways including transcription, metabolic and immune regulation in cancer cells.•This review highlight most recent understanding of mechanisms by which O-GlcNAcylation regulates cancer cell signaling.

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Collaboration types
Domestic collaboration
Web of Science research areas
Cell Biology
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