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https://www.readbyqxmd.com/read/28427939/nrage-induces-%C3%AE-catenin-arm-o-glcnacylation-and-negatively-regulates-wnt-signaling
#1
Yuxin Chen, Lei Jin, Bin Xue, Dong Jin, Fenyong Sun, Chuanjun Wen
The Wnt pathway is crucial for animal development, as well as tumor formation. Understanding the regulation of Wnt signaling will help to elucidate the mechanism of the cell cycle, cell differentiation and tumorigenesis. It is generally accepted that in response to Wnt signals, β-catenin accumulates in the cytoplasm and is imported into the nucleus where it recruits LEF/TCF transcription factors to activate the expression of target genes. In this study, we report that human NRAGE, a neurotrophin receptor p75 (p75NTR) binding protein, markedly suppresses the expression of genes activated by the Wnt pathway...
April 17, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28427012/label-free-electrochemical-biosensing-of-small-molecule-inhibition-on-o-glcnac-glycosylation
#2
Yu Yang, Yuxin Gu, Bin Wan, Xiaomin Ren, Liang-Hong Guo
O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) plays a critical role in modulating protein function in many cellular processes and human diseases such as Alzheimer's disease and type II diabetes, and has emerged as a promising new target. Specific inhibitors of OGT could be valuable tools to probe the biological functions of O-GlcNAcylation, but a lack of robust nonradiometric assay strategies to detect glycosylation, has impeded efforts to identify such compounds. Here we have developed a novel label-free electrochemical biosensor for the detection of peptide O-GlcNAcylation using protease-protection strategy and electrocatalytic oxidation of tyrosine mediated by osmium bipyridine as a signal reporter...
April 12, 2017: Biosensors & Bioelectronics
https://www.readbyqxmd.com/read/28416608/hyper-o-glcnacylation-activates-nf-%C3%AE%C2%BAb-signaling-through-interplay-with-phosphorylation-and-acetylation
#3
Zhiyuan Ma, Robert J Chalkley, Keith Vosseller
O-GlcNAcylation is the covalent addition of an O-linked β-N-acetylglucosamine (O-GlcNAc) sugar moiety to hydroxyl groups of serine/threonine residues of cytosolic and nuclear proteins. O-GlcNAcylation, analogous to phosphorylation, plays critical roles in gene expression through direct modification of transcription factors such as NF-κB. Aberrantly increased NF-κB O-GlcNAcylation has been linked to NF-κB constitutive activation and cancer development. Therefore, it is of a great biological and clinical significance to dissect the molecular mechanisms that tune NF-κB activity...
April 17, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28411811/a-novel-strategy-for-global-mapping-of-o-glcnac-proteins-and-peptides-using-selective-enzymatic-deglycosylation-hilic-enrichment-and-mass-spectrometry-identification
#4
Bingquan Shen, Wanjun Zhang, Zhaomei Shi, Fang Tian, Yulin Deng, Changqing Sun, Guangshun Wang, Weijie Qin, Xiaohong Qian
O-GlcNAcylation is a kind of dynamic O-linked glycosylation of nucleocytoplasmic and mitochondrial proteins. It serves as a major nutrient sensor to regulate numerous biological processes including transcriptional regulation, cell metabolism, cellular signaling, and protein degradation. Dysregulation of cellular O-GlcNAcylated levels contributes to the etiologies of many diseases such as diabetes, neurodegenerative disease and cancer. However, deeper insight into the biological mechanism of O-GlcNAcylation is hampered by its extremely low stoichiometry and the lack of efficient enrichment approaches for large-scale identification by mass spectrometry...
July 1, 2017: Talanta
https://www.readbyqxmd.com/read/28408494/o-glcnacylation-and-cardiovascular-disease
#5
REVIEW
JaLessa N Wright, Helen E Collins, Adam R Wende, John C Chatham
The post-translational modification of serine and threonine residues of proteins found in numerous subcellular locations by O-linked N-acetylglucosamine (O-GlcNAc) is emerging as a key mediator of many cardiovascular pathophysiological processes. Early studies implicated increased protein O-GlcNAcylation as contributing to the cardiovascular complications associated with diabetes, whereas subsequent studies demonstrated that acute increases in O-GlcNAc levels were protective against ischemia/reperfusion injury...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28408483/o-glcnac-cycling-and-the-regulation-of-nucleocytoplasmic-dynamics
#6
REVIEW
Moriah Eustice, Michelle R Bond, John A Hanover
The dynamic carbohydrate post-translational modification (PTM) O-linked β-N-acetyl glucosamine (O-GlcNAc) is found on thousands of proteins throughout the nucleus and cytoplasm, and rivals phosphorylation in terms of the number of substrates and pathways influenced. O-GlcNAc is highly conserved and essential in most organisms, with disruption of O-GlcNAc cycling linked to diseases ranging from cancer to neurodegeneration. Nuclear pore proteins were the first identified O-GlcNAc-modified substrates, generating intense and ongoing interest in understanding the role of O-GlcNAc cycling in nuclear pore complex structure and function...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28408480/eogt-and-o-glcnac-on-secreted-and-membrane-proteins
#7
REVIEW
Shweta Varshney, Pamela Stanley
Here, we describe a recently discovered O-GlcNAc transferase termed EOGT for EGF domain-specific O-GlcNAc transferase. EOGT transfers GlcNAc (N-acetylglucosamine) to Ser or Thr in secreted and membrane proteins that contain one or more epidermal growth factor-like repeats with a specific consensus sequence. Thus, EOGT is distinct from OGT, the O-GlcNAc transferase, that transfers GlcNAc to Ser/Thr in proteins of the cytoplasm or nucleus. EOGT and OGT are in separate cellular compartments and have mostly distinct substrates, although both can act on cytoplasmic (OGT) and lumenal (EOGT) domains of transmembrane proteins...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28408476/ogt-a-short-overview-of-an-enzyme-standing-out-from-usual-glycosyltransferases
#8
REVIEW
Moyira Aquino-Gil, Annick Pierce, Yobana Perez-Cervera, Edgar Zenteno, Tony Lefebvre
O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28408473/o-glcnacylation-and-chromatin-remodeling-in-mammals-an-up-to-date-overview
#9
REVIEW
Maïté Leturcq, Tony Lefebvre, Anne-Sophie Vercoutter-Edouart
Post-translational modifications of histones and the dynamic DNA methylation cycle are finely regulated by a myriad of chromatin-binding factors and chromatin-modifying enzymes. Epigenetic modifications ensure local changes in the architecture of chromatin, thus controlling in fine the accessibility of the machinery of transcription, replication or DNA repair to the chromatin. Over the past decade, the nutrient-sensor enzyme O-GlcNAc transferase (OGT) has emerged as a modulator of chromatin remodeling. In mammals, OGT acts either directly through dynamic and reversible O-GlcNAcylation of histones and chromatin effectors, or in an indirect manner through its recruitment into chromatin-bound multiprotein complexes...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28408472/the-sweet-side-of-the-cell-cycle
#10
REVIEW
Ee Phie Tan, Francesca E Duncan, Chad Slawson
Cell division (mitosis) and gamete production (meiosis) are fundamental requirements for normal organismal development. The mammalian cell cycle is tightly regulated by different checkpoints ensuring complete and precise chromosomal segregation and duplication. In recent years, researchers have become increasingly interested in understanding how O-GlcNAc regulates the cell cycle. The O-GlcNAc post-translation modification is an O-glycosidic bond of a single β-N-acetylglucosamine sugar to serine/threonine residues of intracellular proteins...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28395734/o-glcnac-on-notch1-egf-repeats-regulates-ligand-induced-notch-signaling-and-vascular-development-in-mammals
#11
Shogo Sawaguchi, Shweta Varshney, Mitsutaka Ogawa, Yuta Sakaidani, Hirokazu Yagi, Kyosuke Takeshita, Toyoaki Murohara, Koichi Kato, Subha Sundaram, Pamela Stanley, Tetsuya Okajima
The glycosyltransferase EOGT transfers O-GlcNAc to a consensus site in epidermal growth factor-like (EGF) repeats of a limited number of secreted and membrane proteins, including Notch receptors. In EOGT-deficient cells, the binding of DLL1 and DLL4, but not JAG1, canonical Notch ligands was reduced, and ligand-induced Notch signaling was impaired. Mutagenesis of O-GlcNAc sites on NOTCH1 also resulted in decreased binding of DLL4. EOGT functions were investigated in retinal angiogenesis that depends on Notch signaling...
April 11, 2017: ELife
https://www.readbyqxmd.com/read/28395449/-o-glcnac-glycosylation-influences-the-biological-behaviors-and-etoposide-induced-apoptosis-of-nalm-6-cells
#12
B Zhang, D Li, Q Shi, X L Ju
Objective: To explore the effects of O-GlcNAc glycosylation and its key enzyme OGT on the biological behaviors and etoposide (Vp16) -induced apoptosis of Nalm-6 cells. Methods: Low O-GlcNAc modified Nalm-6 cells model was established with Alloxan, an inhibitor of OGT. The influence of Alloxan on Nalm-6 cells proliferation was checked by CCK-8 assay, apoptosis and cell cycle by flow cytometry. Nalm-6 cells were treated with different concentrations of Vp16 for 12 h, and then the O-GlcNAc level and the expressions of OGT were examined by Western blot...
March 14, 2017: Zhonghua Xue Ye Xue za Zhi, Zhonghua Xueyexue Zazhi
https://www.readbyqxmd.com/read/28347804/o-glcnac-transferase-promotes-fatty-liver-associated-liver-cancer-through-inducing-palmitic-acid-and-activating-endoplasmic-reticulum-stress
#13
Weiqi Xu, Xiang Zhang, Jian-Lin Wu, Li Fu, Ken Liu, Dabin Liu, George Gong Chen, Paul Bo-San Lai, Nathalie Wong, Jun Yu
BACKGROUND & AIMS: O-GlcNAc transferase (OGT) is a unique glycosyltransferase involved in metabolic reprogramming. We investigated the functional role of OGT in non-alcoholic fatty liver disease-associated hepatocellular carcinoma (NAFLD-HCC). METHODS: The biological function of OGT in NAFLD-HCC was determined by gain- or loss- of OGT functional assays in vitro and in nude mice. OGT target factors and pathways were identified by liquid chromatography-tandem mass spectrometry (LC-MS), promoter luciferase assay, DNA binding activity assay and Western blot...
March 24, 2017: Journal of Hepatology
https://www.readbyqxmd.com/read/28346407/insights-into-activity-and-inhibition-from-the-crystal-structure-of-human-o-glcnacase
#14
Nathaniel L Elsen, Sangita B Patel, Rachael E Ford, Dawn L Hall, Fred Hess, Hari Kandula, Maria Kornienko, John Reid, Harold Selnick, Jennifer M Shipman, Sujata Sharma, Kevin J Lumb, Stephen M Soisson, Daniel J Klein
O-GlcNAc hydrolase (OGA) catalyzes removal of βα-linked N-acetyl-D-glucosamine from serine and threonine residues. We report crystal structures of Homo sapiens OGA catalytic domain in apo and inhibited states, revealing a flexible dimer that displays three unique conformations and is characterized by subdomain α-helix swapping. These results identify new structural features of the substrate-binding groove adjacent to the catalytic site and open new opportunities for structural, mechanistic and drug discovery activities...
March 27, 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/28346405/structural-and-functional-insight-into-human-o-glcnacase
#15
Christian Roth, Sherry Chan, Wendy A Offen, Glyn R Hemsworth, Lianne I Willems, Dustin T King, Vimal Varghese, Robert Britton, David J Vocadlo, Gideon J Davies
O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value...
March 27, 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/28339907/o-linked-%C3%AE-n-acetylglucosamine-modification-of-proteins-is-essential-for-foot-process-maturation-and-survival-in-podocytes
#16
Shinya Ono, Shinji Kume, Mako Yasuda-Yamahara, Kosuke Yamahara, Naoko Takeda, Masami Chin-Kanasaki, Hisazumi Araki, Osamu Sekine, Hideki Yokoi, Masashi Mukoyama, Takashi Uzu, Shin-Ichi Araki, Hiroshi Maegawa
Background.: O-linked β- N -acetylglucosamine modification O-GlcNAcylation) is a post-translational modification of intracellular proteins, serving as a nutrient sensor. Growing evidence has demonstrated its physiological and pathological importance in various mammalian tissues. This study examined the physiological role of O-GlcNAcylation in podocyte function and development. Methods.: O-GlcNAc transferase (Ogt) is a critical enzyme for O-GlcNAcylation and resides on the X chromosome...
February 27, 2017: Nephrology, Dialysis, Transplantation
https://www.readbyqxmd.com/read/28336748/the-sweet-side-of-ampk-signaling-regulation-of-gfat1
#17
John W Scott, Jonathan S Oakhill
Maintaining a steady balance between nutrient supply and energy demand is essential for all living organisms and is achieved through the dynamic control of metabolic processes that produce and consume adenosine-5'-triphosphate (ATP), the universal currency of energy in all cells. A key sensor of cellular energy is the adenosine-5'-monophosphate (AMP)-activated protein kinase (AMPK), which is the core component of a signaling network that regulates energy and nutrient metabolism. AMPK is activated by metabolic stresses that decrease cellular ATP, and functions to restore energy balance by orchestrating a switch in metabolism away from anabolic pathways toward energy-generating catabolic processes...
March 23, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28319083/structures-of-human-o-glcnacase-and-its-complexes-reveal-a-new-substrate-recognition-mode
#18
Baobin Li, Hao Li, Lei Lu, Jiaoyang Jiang
Human O-GlcNAcase (hOGA) is the unique enzyme responsible for the hydrolysis of the O-linked β-N-acetyl glucosamine (O-GlcNAc) modification, an essential protein glycosylation event that modulates the function of numerous cellular proteins in response to nutrients and stress. Here we report crystal structures of a truncated hOGA, which comprises the catalytic and stalk domains, in apo form, in complex with an inhibitor, and in complex with a glycopeptide substrate. We found that hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft...
April 2017: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/28314751/identification-of-glycopeptides-as-post-translationally-modified-neoantigens-in-leukemia
#19
Stacy A Malaker, Sarah A Penny, Lora G Steadman, Paisley T Myers, Justin Loke, Manoj Raghavan, Dina L Bai, Jeffery Shabanowitz, Donald Hunt, Mark Cobbold
Leukemias are highly immunogenic but have a low mutational load, providing few mutated peptide targets. Thus, the identification of alternative neoantigens is a pressing need. Here, we identify 36 MHC class I-associated peptide antigens with O-linked β-N-acetylglucosamine (O-GlcNAc) modifications as candidate neoantigens, using three experimental approaches. Thirteen of these peptides were also detected with disaccharide units on the same residues and two contain either mono- and/or di-methylated arginine residues...
March 17, 2017: Cancer Immunology Research
https://www.readbyqxmd.com/read/28302723/identification-and-characterization-of-a-missense-mutation-in-the-o-glcnac-transferase-gene-that-segregates-with-x-linked-intellectual-disability
#20
Krithika Vaidyanathan, Tejasvi Niranjan, Nithya Selvan, Chin Fen Teo, Melanie May, Sneha Patel, Brent Weatherly, Cindy Skinner, John Opitz, John Carey, David Viskochil, Jozef Gecz, Marie Shaw, Yunhui Peng, Emil Alexov, Tao Wang, Charles Schwartz, Lance Wells
O-GlcNAc is a regulatory post-translational modification of nucleocytoplasmic proteins that has been implicated in multiple biological processes including transcription. In humans, single genes encode enzymes for its attachment [O-GlcNAc transferase (OGT)] and removal [O-GlcNAcase (OGA)]. An X-chromosome exome screen identified a missense mutation, that encodes an amino acid in the tetratricopeptide repeat, in OGT (759G>T (p.L254F)) that segregates with X-linked intellectual disability (XLID) in an affected family...
March 16, 2017: Journal of Biological Chemistry
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