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https://www.readbyqxmd.com/read/28922739/o-glcnac-transferase-regulates-transcriptional-activity-of-human-oct4
#1
Sandii Constable, Jae-Min Lim, Krithika Vaidyanathan, Lance Wells
O-linked β-N-acetylglucosamine (O-GlcNAc) is a single sugar modification found on many different classes of nuclear and cytoplasmic proteins. Addition of this modification, by the enzyme O-linked N-acetylglucosamine transferase (OGT), is dynamic and inducible. One major class of proteins modified by O-GlcNAc is transcription factors. O-GlcNAc regulates transcription factor properties through a variety of different mechanisms including localization, stability and transcriptional activation. Maintenance of embryonic stem (ES) cell pluripotency requires tight regulation of several key transcription factors, many of which are modified by O-GlcNAc...
October 1, 2017: Glycobiology
https://www.readbyqxmd.com/read/28910574/o-glcnacylation-of-boundary-element-associated-factor-beaf-32-in-drosophila-melanogaster-correlates-with-active-histone-marks-at-the-promoters-of-its-target-genes
#2
Debaditya De, Satish Kallappagoudar, Jae-Min Lim, Rashmi U Pathak, Rakesh K Mishra
Boundary Element-Associated Factor 32 (BEAF 32) is a sequence specific DNA binding protein involved in functioning of chromatin domain boundaries in Drosophila. Several studies also show it to be involved in transcriptional regulation of a large number of genes, many of which are annotated to have cell cycle, development and differentiation related function. Since post-translational modifications (PTMs) of proteins add to their functional capacity, we investigated the PTMs on BEAF 32. The protein is known to be phosphorylated and O-GlcNAcylated...
September 14, 2017: Nucleus
https://www.readbyqxmd.com/read/28903979/calcium-dependent-o-glcnac-signaling-drives-liver-autophagy-in-adaptation-to-starvation
#3
Hai-Bin Ruan, Yina Ma, Sara Torres, Bichen Zhang, Colleen Feriod, Ryan M Heck, Kevin Qian, Minnie Fu, Xiuqi Li, Michael H Nathanson, Anton M Bennett, Yongzhan Nie, Barbara E Ehrlich, Xiaoyong Yang
Starvation induces liver autophagy, which is thought to provide nutrients for use by other organs and thereby maintain whole-body homeostasis. Here we demonstrate that O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is required for glucagon-stimulated liver autophagy and metabolic adaptation to starvation. Genetic ablation of OGT in mouse livers reduces autophagic flux and the production of glucose and ketone bodies. Upon glucagon-induced calcium signaling, calcium/calmodulin-dependent kinase II (CaMKII) phosphorylates OGT, which in turn promotes O-GlcNAc modification and activation of Ulk proteins by potentiating AMPK-dependent phosphorylation...
September 13, 2017: Genes & Development
https://www.readbyqxmd.com/read/28894244/impact-of-protein-o-glcnacylation-on-neural-tube-malformation-in-diabetic-embryopathy
#4
Gyuyoup Kim, Lixue Cao, E Albert Reece, Zhiyong Zhao
Diabetes mellitus in early pregnancy can cause neural tube defects (NTDs) in embryos by perturbing protein activity, causing cellular stress, and increasing programmed cell death (apoptosis) in the tissues required for neurulation. Hyperglycemia augments a branch pathway in glycolysis, the hexosamine biosynthetic pathway (HBP), to increase uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc). GlcNAc can be added to proteins by O-GlcNAc transferase (OGT) to regulate protein activity. In the embryos of diabetic mice, OGT is highly activated in association with increases in global protein O-GlcNAcylation...
September 11, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28886091/a-study-of-the-structural-properties-of-sites-modified-by-the-o-linked-6-n-acetylglucosamine-transferase
#5
Thiago Britto-Borges, Geoffrey J Barton
Protein O-GlcNAcylation (O-GlcNAc) is an essential post-translational modification (PTM) in higher eukaryotes. The O-linked β-N-acetylglucosamine transferase (OGT), targets specific Serines and Threonines (S/T) in intracellular proteins. However, unlike phosphorylation, fewer than 25% of known O-GlcNAc sites match a clear sequence pattern. Accordingly, the three-dimensional structures of O-GlcNAc sites were characterised to investigate the role of structure in molecular recognition. From 1,584 O-GlcNAc sites in 620 proteins, 143 were mapped to protein structures determined by X-ray crystallography...
2017: PloS One
https://www.readbyqxmd.com/read/28861343/aralia-elata-inhibits-neurodegeneration-by-downregulating-o-glcnacylation-of-nf-%C3%AE%C2%BAb-in-diabetic-mice
#6
Seong-Jae Kim, Min-Jun Kim, Mee-Young Choi, Yoon-Sook Kim, Ji-Myong Yoo, Eun-Kyung Hong, Sunmi Ju, Wan-Sung Choi
AIM: To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice. METHODS: C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM). Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined...
2017: International Journal of Ophthalmology
https://www.readbyqxmd.com/read/28844813/measurement-of-o-glcnacylated-endothelial-nitric-oxide-synthase-by-using-2-5-adp-sepharose-pull-down-assay
#7
Yang Long, Jianghong Yan, Suxin Luo, Zhenguo Liu, Yong Xia
Endothelial nitric oxide synthase (eNOS) plays central roles in cardiovascular regulation and disease. eNOS function is critically affected by O-linked N-acetylglucosamine (O-GlcNAc) modification. The present method for measuring O-GlcNAcylated eNOS relies on immunoprecipitation. Such method exhibits low detection efficiency and is also costly. We here report a simplified assay by employing the high binding affinity of eNOS with the 2',5'-ADP-Sepharose resins. Together with the O-GlcNAc antibody, this assay readily allows the detection of O-GlcNAcylated eNOS in both cultured endothelial cells and rat vascular tissues...
August 24, 2017: Analytical Biochemistry
https://www.readbyqxmd.com/read/28843855/metformin-protects-against-retinal-cell-death-in-diabetic-mice
#8
Yoon Sook Kim, Minjun Kim, Mee Young Choi, Dong Hoon Lee, Gu Seob Roh, Hyun Joon Kim, Sang Soo Kang, Gyeong Jae Cho, Seong-Jae Kim, Ji-Myong Yoo, Wan Sung Choi
Retinal degeneration is an early feature of diabetic retinopathy, the major cause of blindness in the developed world. Here we investigated how the widely used antidiabetic drug metformin reduces retinal injury in diabetic mice. Metformin was orally administered to control mice or mice with streptozotocin-induced diabetes. Western blot analysis showed that levels of O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and other related proteins such as carbohydrate-responsive element-binding protein (ChREBP) and thioredoxin-interacting protein (TXNIP) were significantly increased, and nuclear factor kappaB (NF-κB) and poly (ADP-ribose) polymerase (PARP) were activated in the diabetic retinas or retinal pigment epithelial (RPE) cells exposed to high glucose compared to controls...
August 23, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28808029/elucidating-crosstalk-mechanisms-between-phosphorylation-and-o-glcnacylation
#9
Aneika C Leney, Dris El Atmioui, Wei Wu, Huib Ovaa, Albert J R Heck
Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time. Unraveling this complex PTM code is one of the great challenges in molecular biology. Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other. We demonstrate two generic crosstalk mechanisms. First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation...
August 14, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28802580/suppressive-role-of-ogt-mediated-o-glcnacylation-of-bap1-in-retinoic-acid-signaling
#10
Seungtae Moon, Yong-Kyu Lee, Sang-Wang Lee, Soo-Jong Um
BRCA1-associated protein 1 (BAP1) has been implicated in diverse biological functions, including tumor suppression. However, its regulation via glycosylation and its role in embryonic stem (ES) cells are poorly defined. BAP1 was recently reported to interact with O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT). Here, we confirmed the physical interaction and investigated its functional significance. The O-GlcNAcylation of BAP1, which requires OGT, was examined in vivo and in vitro, and was proven using alloxan, an OGT inhibitor...
August 10, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28793197/glycosylation-with-o-linked-%C3%AE-n-acetylglucosamine-o-glcnac-induces-vascular-dysfunction-via-production-of-superoxide-anion-reactive-oxygen-species
#11
Leonardo Souza-Silva, Rhéure Alves-Lopes, Jéssica Silva Miguez, Vanessa Dela Justina, Karla Bianca Neves, Fabíola Leslie Mestriner, Rita C Tostes, Fernanda Regina Giachini, Victor V Lima
Overproduction of superoxide anion (•O2-) and O-linked β-N-acetylglucosamine (O-GlcNAc)-modification in the vascular system are contributors to endothelial dysfunction. This study tested the hypothesis that increased levels of O-GlcNAc-modified proteins contribute to •O2- production via activation of NADPH oxidase, resulting in impaired vasodilation. Rat aortic segments and vascular smooth muscle cell (VSMCs) were incubated with vehicle (methanol) or PUGNAc (100 µM). PUGNAc produced a time-dependent increase in O-GlcNAc levels in VSMC and decreased endothelium-dependent relaxation, which was prevented by apocynin and Tiron, suggesting that •O2- contributes to endothelial dysfunction under augmented O-GlcNAc levels...
August 9, 2017: Canadian Journal of Physiology and Pharmacology
https://www.readbyqxmd.com/read/28768194/a-conserved-splicing-silencer-dynamically-regulates-o-glcnac-transferase-intron-retention-and-o-glcnac-homeostasis
#12
Sung-Kyun Park, Xiaorong Zhou, Kathryn E Pendleton, Olga V Hunter, Jennifer J Kohler, Kathryn A O'Donnell, Nicholas K Conrad
Modification of nucleocytoplasmic proteins with O-GlcNAc regulates a wide variety of cellular processes and has been linked to human diseases. The enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) add and remove O-GlcNAc, but the mechanisms regulating their expression remain unclear. Here, we demonstrate that retention of the fourth intron of OGT is regulated in response to O-GlcNAc levels. We further define a conserved intronic splicing silencer (ISS) that is necessary for OGT intron retention. Deletion of the ISS in colon cancer cells leads to increases in OGT, but O-GlcNAc homeostasis is maintained by concomitant increases in OGA protein...
August 1, 2017: Cell Reports
https://www.readbyqxmd.com/read/28760965/quantitative-time-resolved-chemoproteomics-reveals-that-stable-o-glcnac-regulates-box-c-d-snornp-biogenesis
#13
Wei Qin, Pinou Lv, Xinqi Fan, Baiyi Quan, Yuntao Zhu, Ke Qin, Ying Chen, Chu Wang, Xing Chen
O-linked GlcNAcylation (O-GlcNAcylation), a ubiquitous posttranslational modification on intracellular proteins, is dynamically regulated in cells. To analyze the turnover dynamics of O-GlcNAcylated proteins, we developed a quantitative time-resolved O-linked GlcNAc proteomics (qTOP) strategy based on metabolic pulse-chase labeling with an O-GlcNAc chemical reporter and stable isotope labeling with amino acids in cell culture (SILAC). Applying qTOP, we quantified the turnover rates of 533 O-GlcNAcylated proteins in NIH 3T3 cells and discovered that about 14% exhibited minimal removal of O-GlcNAc or degradation of protein backbones...
August 15, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28760863/acute-increases-in-protein-o-glcnacylation-dampen-epileptiform-activity-in-hippocampus
#14
Luke T Stewart, Anas U Khan, Kai Wang, Diana Pizarro, Sandipan Pati, Susan C Buckingham, Michelle L Olsen, John C Chatham, Lori L McMahon
O-GlcNAcylation is a ubiquitous and dynamic post-translational modification involving the O-linkage of β-N-acetylglucosamine to serine/threonine residues of membrane, cytosolic, and nuclear proteins. This modification is similar to phosphorylation and regarded as a key regulator of cell survival and homeostasis. Previous studies have shown that phosphorylation of serine residues on synaptic proteins is a major regulator of synaptic strength and long-term plasticity, suggesting that O-GlcNAcylation of synaptic proteins is likely as important as phosphorylation; however, few studies have investigated its role in synaptic efficacy...
August 23, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28742148/hijacking-of-the-o-glcnaczyme-complex-by-the-htlv-1-tax-oncoprotein-facilitates-viral-transcription
#15
Damien Groussaud, Mostafa Khair, Armelle I Tollenaere, Laetitia Waast, Mei-Shiue Kuo, Marianne Mangeney, Christophe Martella, Yann Fardini, Solène Coste, Mouloud Souidi, Laurence Benit, Claudine Pique, Tarik Issad
The viral Tax oncoprotein plays a key role in both Human T-cell lymphotropic virus type 1 (HTLV-1)-replication and HTLV-1-associated pathologies, notably adult T-cell leukemia. Tax governs the transcription from the viral 5'LTR, enhancing thereby its own expression, via the recruitment of dimers of phosphorylated CREB to cAMP-response elements located within the U3 region (vCRE). In addition to phosphorylation, CREB is also the target of O-GlcNAcylation, another reversible post-translational modification involved in a wide range of diseases, including cancers...
July 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28739801/sustained-o-glcnacylation-reprograms-mitochondrial-function-to-regulate-energy-metabolism
#16
Ee Phie Tan, Steven R McGreal, Stefan Graw, Robert Tessman, Scott J Koppel, Pramod Dhakal, Zhen Zhang, Miranda Machacek, Natasha E Zachara, Devin C Koestler, Kenneth R Peterson, John P Thyfault, Russell H Swerdlow, Partha Krishnamurthy, Luciano DiTacchio, Udayan Apte, Chad Slawson
Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions. Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function. Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function...
September 8, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28724388/o-glcnac-regulation-of-autophagy-and-%C3%AE-synuclein-homeostasis-implications-for-parkinson-s-disease
#17
Willayat Y Wani, Xiaosen Ouyang, Gloria A Benavides, Matthew Redmann, Stacey S Cofield, John J Shacka, John C Chatham, Victor Darley-Usmar, Jianhua Zhang
Post-translational modification on protein Ser/Thr residues by O-linked attachment of ß-N-acetyl-glucosamine (O-GlcNAcylation) is a key mechanism integrating redox signaling, metabolism and stress responses. One of the most common neurodegenerative diseases that exhibit aberrant redox signaling, metabolism and stress response is Parkinson's disease, suggesting a potential role for O-GlcNAcylation in its pathology. To determine whether abnormal O-GlcNAcylation occurs in Parkinson's disease, we analyzed lysates from the postmortem temporal cortex of Parkinson's disease patients and compared them to age matched controls and found increased protein O-GlcNAcylation levels...
July 19, 2017: Molecular Brain
https://www.readbyqxmd.com/read/28722313/cellular-glycosylation-senses-metabolic-changes-and-modulates-cell-plasticity-during-epithelial-to-mesenchymal-transition
#18
Patricia Carvalho-Cruz, Frederico Alisson-Silva, Adriane R Todeschini, Wagner B Dias
Epithelial to mesenchymal transition (EMT) is a developmental program reactivated by tumor cells that leads to the switch from epithelial to mesenchymal phenotype. During EMT, cells are transcriptionally regulated to decrease E-cadherin expression while expressing mesenchymal markers such as vimentin, fibronectin, and N-cadherin. Growing body of evidences suggest that cells engaged in EMT undergo a metabolic reprograming process, redirecting glucose flux toward hexosamine biosynthesis pathway (HBP), which fuels aberrant glycosylation patterns that are extensively observed in cancer cells...
July 19, 2017: Developmental Dynamics: An Official Publication of the American Association of Anatomists
https://www.readbyqxmd.com/read/28713921/anti%C3%A2-lung-cancer-effect-of-glucosamine-by-suppressing-the-phosphorylation-of-foxo
#19
Zhanwu Yu, Yinghua Ju, Hongxu Liu
Lung cancer is the most common cause of cancer‑associated mortality worldwide, and glucosamine has the potential to exhibit antitumor activity. To reveal its anti‑lung cancer mechanism, the present study investigated the effect of glucosamine on the transcriptional activity of forkhead box O (FOXO)1 and FOXO3, and associated signal transduction pathways in A549 cells. An MTT assay was performed to investigate cell viability and immunoblotting was performed to detect protein levels of FOXO1/3, phosphorylated (p)‑FOXO1/3, AKT, p‑AKT, extracellular signal‑regulated kinase (ERK) and p‑ERK, and the levels of β‑O‑linked N‑acetylglucosamine (O‑GlcNAc)‑modified FOXO1 protein...
September 2017: Molecular Medicine Reports
https://www.readbyqxmd.com/read/28710799/high-glucose-induces-o-glcnac-glycosylation-of-the-vitamin-d-receptor-vdr-in-thp1-cells-and-in-human-macrophages-derived-from-monocytes
#20
Fernando Hernández-Sánchez, Silvia Guzmán-Beltrán, María Teresa Herrera, Yolanda Gonzalez, Manuel Salgado, Guadalupe Fabian, Martha Torres
Chronic hyperglycemia increases the carbon flux through the hexosamine pathway, allowing the accumulation of UDP-GlcNAc. UDP-GlcNAc is the sugar donor for the enzyme-mediated protein glycosylation event known as OGlcNAcylation. This posttranslational modification targets several transcription factors implicated in glucose toxicity, insulin resistance, and diabetes. Vitamin D plays an important role in glucose homeostasis and insulin secretion through transcriptional mechanisms mediated by its receptor (VDR)...
July 15, 2017: Cell Biology International
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