The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities in Drosophila
Sign Up to like & getrecommendations! Published in 2020 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.1912894117
Abstract: Significance O-GlcNAc transferase (OGT) transfers the sugar O-GlcNAc to serine and threonine residues of target proteins, a process known as O-GlcNAcylation. Using Drosophila as an animal model, we identify the protein kinase Hipk as a… read more here.
Keywords: protein stability; human hipk2; ogt; hipk ... See more keywords
Ogt Demonstrated Conspicuous Clinical Significance in Cancers, from Pan-Cancer to Small-Cell Lung Cancer
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DOI: 10.1155/2022/2010341
Abstract: The clinical progression of small-cell lung cancer (SCLC) remains pessimistic. The aim of the present study was to promote the understanding of the clinical significance and mechanism of O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) in SCLC.… read more here.
Keywords: clinical significance; sclc; small cell; ogt ... See more keywords
Pancreatic Beta Cell O-GlcNAc Transferase Overexpression Increases Susceptibility to Streptozotocin- and High-Fat Diet–Induced Diabetes in Female Mice
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DOI: 10.2337/db18-83-or
Abstract: The nutrient-sensor O-GlcNAc transferase (OGT), the sole enzyme that adds an O-GlcNAc-modification onto proteins, was shown to regulate β-cell survival and function as β-cell deletion of OGT induces diabetes and islet failure in mice. We… read more here.
Keywords: cre ogtoe; induced diabetes; rip cre; ogt ... See more keywords
DNA Polymerase Iota Promotes Esophageal Squamous Cell Carcinoma Proliferation Through Erk-OGT-Induced G6PD Overactivation
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DOI: 10.3389/fonc.2021.706337
Abstract: Esophageal squamous cell carcinoma (ESCC) is one of the most lethal cancers with rapid progression and a high mortality rate. Our previous study demonstrated that DNA polymerase iota (Pol ι) is overexpressed in ESCC tumors… read more here.
Keywords: erk; glcnacylation; proliferation; ogt ... See more keywords
OGT binds a conserved C-terminal domain of TET1 to regulate TET1 activity and function in development
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DOI: 10.7554/elife.34870
Abstract: TET enzymes convert 5-methylcytosine to 5-hydroxymethylcytosine and higher oxidized derivatives. TETs stably associate with and are post-translationally modified by the nutrient-sensing enzyme OGT, suggesting a connection between metabolism and the epigenome. Here, we show for… read more here.
Keywords: function development; tet1 activity; ogt; tet1 ... See more keywords