Nutrient regulation of signaling and transcription.
TLDR
This review will present an overview of the current understanding of O-GlcNAc's regulation, functions, and roles in chronic diseases of aging.About:
This article is published in Journal of Biological Chemistry.The article was published on 2019-02-15 and is currently open access. It has received 235 citations till now. The article focuses on the topics: Phosphorylation & Secretory pathway.read more
Citations
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Global view of human protein glycosylation pathways and functions
TL;DR: This work predicts that use of (single-cell) transcriptomics, genetic screens, genetic engineering of cellular glycosylation capacities and custom design of glycoprotein therapeutics are advancements that will ignite wider integration of gly cosylation in general cell biology.
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Glycosylation in the Era of Cancer-Targeted Therapy: Where Are We Heading?
TL;DR: This review provides insights on the impact of glycosylation in cancer biology and its influence in the current approaches of targeted cancer therapies in the clinical setting, outlining potential applications of glycan-based biomarkers for patient stratification and strategies for improving personalized cancer treatment.
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Congenital disorders of glycosylation.
TL;DR: Carohydrate deficient transferrin (CDT) and protein-linked glycan analysis with mass spectrometry can diagnose some subtypes of congenital disorders of glycosylation (CDG), while many currently rely on massively parallel genomic sequencing for diagnosis.
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Metabolic reprogramming and epigenetic modifications on the path to cancer.
TL;DR: In this article, the authors focus on how metabolic reprogramming of tumor cells and immune cells reshapes epigenetic alterations, in particular the acetylation and methylation of histone proteins and DNA, and discuss other eminent metabolic modifications such as, succinylation, hydroxybutyrylation, and lactylation.
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Role of O-Linked N-Acetylglucosamine Protein Modification in Cellular (Patho)Physiology.
TL;DR: The current understanding of the processes involved in regulating O- GlcNAc turnover, the role of O-GlcNAcylation in regulating cellular physiology, and how dysregulation in O- GloverNAc cycling contributes to pathophysiological processes are outlined.
References
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Cycling of O-linked β- N -acetylglucosamine on nucleocytoplasmic proteins
TL;DR: Emerging data indicate that O-GlcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration.
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Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.
TL;DR: Recent glycomic analyses have shown that O-GlcNAcylation has surprisingly extensive cross talk with phosphorylation, where it serves as a nutrient/stress sensor to modulate signaling, transcription, and cytoskeletal functions.
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Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
Xue Liang Du,Diane Edelstein,Luciano Rossetti,I. G. Fantus,Howard J. Goldberg,Fuad N. Ziyadeh,Jie Wu,Michael Brownlee +7 more
TL;DR: Hyperglycemia-induced mitochondrial superoxide overproduction increases hexosamine synthesis and O-glycosylation of Sp1, which activates expression of genes that contribute to the pathogenesis of diabetic complications.
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Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance.
TL;DR: It is indicated that a unique metabolic pathway exists in adipocytes that mediates desensitization of the insulin-responsive GTS, and that an early step in this pathway involves the conversion of fructose 6-phosphate to glucosamine 6- phosphate by the first and rate-limiting enzyme of the hexosamine pathway, glutamine:fructose-6-ph phosphate amidotransferase.
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Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.
C. R. Torres,Gerald W. Hart +1 more
TL;DR: Dramatic differences in the amounts and distribution of terminal GlcNAc residues on phenotypically different lymphocyte populations are described, but the presence of a novel protein-saccharide linkage, which is present on numerous lymphocyte proteins, is described.