O-GlcNAc Transferase Is Involved in Glucocorticoid Receptor-mediated Transrepression [PDF]
Journal of Biological Chemistry, 2012 Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression. Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated. Here we report that OGT is an important component of GR-mediated transrepression.
Min-Dian, Li +8 more
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Endoplasmic Reticulum Export of GPI-Anchored Proteins [PDF]
, 2019 Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus ...
López Martín, Sergio +3 more
core +1 more source
The Making of a Sweet Modification: Structure and Function of O-GlcNAc Transferase [PDF]
Journal of Biological Chemistry, 2014 O-GlcNAc transferase is an essential mammalian enzyme responsible for transferring a single GlcNAc moiety from UDP-GlcNAc to specific serine/threonine residues of hundreds of nuclear and cytoplasmic proteins. This modification is dynamic and has been implicated in numerous signaling pathways.
John, Janetzko, Suzanne, Walker
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O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease. [PDF]
, 2015 Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies ...
Ambroso, Mark R +8 more
core +2 more sources
Parallel identification of O-GlcNAc-modified proteins from cell lysates [PDF]
, 2004 We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be ...
Ficarro, Scott B. +4 more
core +1 more source
Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase [PDF]
Nature Chemical Biology, 2017 O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is an essential human glycosyltransferase that adds O-GlcNAc modifications to numerous proteins. However, little is known about the mechanism with which OGT recognizes various protein substrates.
Chia-Wei Hu +11 more
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Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase [PDF]
Proceedings of the National Academy of Sciences, 2020 Significance Mammalian cells contain only one glycosyltransferase, OGT, that operates in the nucleus and cytoplasm rather than the secretory pathway. OGT is required for cell proliferation, but a basic unanswered question is which OGT functions are essential.
Zebulon G. Levine +9 more
openaire +3 more sources
Mass Spectrometry in the Elucidation of the Glycoproteome of Bacterial Pathogens [PDF]
, 2010 Presently some three hundred post-translational modifications are known to occur in bacteria in vivo. Many of these modifications play critical roles in the regulation of proteins and control key biological processes.
Graham, Robert L. J., Hess, Sonja
core +1 more source
A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin [PDF]
Chromosoma, 2015 O-linked β-N-Acetylglucosamine (O-GlcNAc) is a posttranslational modification that is catalyzed by O-GlcNAc transferase (Ogt) and found on a plethora of nuclear and cytosolic proteins in animals and plants. Studies in different model organisms revealed that while O-GlcNAc is required for selected processes in Caenorhabditis elegans and Drosophila, it ...
Maria Cristina Gambetta, Jürg Müller
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Glucose and glutamine fuel protein O-GlcNAcylation to control T cell self-renewal and malignancy [PDF]
, 2016 Sustained glucose and glutamine transport are essential for activated T lymphocytes to support ATP and macromolecule biosynthesis. We now show that glutamine and glucose also fuel an indispensible dynamic regulation of intracellular protein O ...
A Boudil +54 more
core +3 more sources