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SUMOylation

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https://www.readbyqxmd.com/read/28319808/identifying-regulatory-posttranslational-modifications-of-pd-l1-a-focus-on-monoubiquitinaton
#1
Henrick Horita, Andy Law, Soonjin Hong, Kim Middleton
A set of high-affinity, high-specificity posttranslational modification (PTM) enrichment tools was developed to generate an unbiased snapshot of four key PTM profiles (tyrosine phosphorylation, acetylation, ubiquitination, and SUMOylation 2/3) for the clinically important protein programmed cell death ligand 1 (PD-L1). The results showed that epidermal growth factor (EGF) treatment induced tyrosine phosphorylation, acetylation, and ubiquitination of PD-L1. Further characterization of EGF-induced PD-L1 ubiquitination revealed a significant increase in mono- and multiubiquitination of PD-L1 that occurred on glycosylated PD-L1...
March 16, 2017: Neoplasia: An International Journal for Oncology Research
https://www.readbyqxmd.com/read/28318385/arsenic-induced-sumoylation-of-mus81-is-involved-in-regulating-genomic-stability
#2
Liyan Hu, Feikun Yang, Lou Lu, Wei Dai
Chronic environmental exposure to metal toxicants such as chromium and arsenic is closely related to the development of several types of common cancers. Genetic and epigenetic studies in the past decade reveal that post-translational modifications of histones play a role in metal carcinogenesis. However, exact molecular mechanisms of metal carcinogenesis remain to be elucidated. In this study we found that As2O3, an environmental metal toxicant, up-regulated overall modifications of many cellular proteins by SUMO2/3...
March 20, 2017: Cell Cycle
https://www.readbyqxmd.com/read/28314856/ubc9-is-required-for-positive-selection-and-late-stage-maturation-of-thymocytes
#3
Aibo Wang, Xiao Ding, Maud Demarque, Xindong Liu, Deng Pan, Huawei Xin, Bo Zhong, Xiaohu Wang, Anne Dejean, Wei Jin, Chen Dong
SUMOylation is an important posttranslational modification that regulates protein function in diverse biological processes. However, its role in early T cell development has not been genetically studied. UBC9 is the only E2 enzyme for all SUMOylation. In this study, by selectively deleting Ubc9 gene in T cells, we have investigated the functional roles of SUMOylation in T cell development. Loss of Ubc9 results in a significant reduction of CD4 and CD8 single-positive lymphocytes in both thymus and periphery...
March 17, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/28289178/proteome-wide-mapping-of-endogenous-sumoylation-sites-in-mouse-testis
#4
Lili Cai, Jun Tu, Lei Song, Zhihua Gao, Kai Li, Yunzhi Wang, Yang Liu, Fan Zhong, Rui Ge, Jun Qin, Chen Ding, Fuchu He
SUMOylation is a reversible post-translational modification involved in various critical biological processes. To date, there is limited approach for endogenous wild-type SUMO-modified peptides enrichment and SUMOylation sites identification. In this study, we generated a high-affinity SUMO1 antibody to facilitate the enrichment of endogenous SUMO1-modified peptides from Trypsin/Lys-C protease digestion. Following secondary Glu-C protease digestion, we identified 53 high-confidence SUMO1-modified sites from mouse testis by using high-resolution mass spectrometry...
March 13, 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28285006/gata5-sumoylation-is-indispensable-for-zebrafish-cardiac-development
#5
Bin Wen, Hao Yuan, Xiaohui Liu, Haihong Wang, Saijuan Chen, Zhu Chen, Hugues de The, Jun Zhou, Jun Zhu
BACKGROUND: SUMOylation is a critical regulatory protein modification in eukaryotic cells and plays a pivotal role in cardiac development and disease. Several cardiac transcription factors are modified by SUMO, but little is known about the impact of SUMOylation on their function during cardiac development. METHODS: We used a zebrafish model to address the impact of SUMOylation on GATA5, an essential transcription factor in zebrafish cardiac development. GATA5 SUMOylation was probed by western blot, the subcellular localization and transcriptional activity of GATA5 mutants were examined by immunostaining and luciferase reporter assay...
March 8, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28284030/sumo-conjugation-a-mechanistic-view
#6
REVIEW
Andrea Pichler, Chronis Fatouros, Heekyoung Lee, Nathalie Eisenhardt
The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate...
March 1, 2017: Biomolecular Concepts
https://www.readbyqxmd.com/read/28280500/post-translational-modifications-in-regulation-of-chloroplast-function-recent-advances
#7
REVIEW
Magda Grabsztunowicz, Minna M Koskela, Paula Mulo
Post-translational modifications (PTMs) of proteins enable fast modulation of protein function in response to metabolic and environmental changes. Phosphorylation is known to play a major role in regulating distribution of light energy between the Photosystems (PS) I and II (state transitions) and in PSII repair cycle. In addition, thioredoxin-mediated redox regulation of Calvin cycle enzymes has been shown to determine the efficiency of carbon assimilation. Besides these well characterized modifications, recent methodological progress has enabled identification of numerous other types of PTMs in various plant compartments, including chloroplasts...
2017: Frontiers in Plant Science
https://www.readbyqxmd.com/read/28277940/a-single-structurally-conserved-sumoylation-site-in-crmp2-controls-nav1-7-function
#8
Erik Thomas Dustrude, Samantha Perez-Miller, Liberty François-Moutal, Aubin Moutal, May Khanna, Rajesh Khanna
The neuronal collapsin response mediator protein 2 (CRMP2) undergoes several posttranslational modifications that codify its functions. Most recently, CRMP2 SUMOylation (addition of small ubiquitin like modifier (SUMO)) was identified as a key regulatory step within a modification program that codes for CRMP2 interaction with, and trafficking of, voltage-gated sodium channel NaV1.7. In this addendum, we illustrate the utility of combining sequence alignment within protein families with structural analysis to identify, from a number of putative SUMOylation sites, those that are most likely to be biologically relevant...
February 28, 2017: Channels
https://www.readbyqxmd.com/read/28275011/ataxin-3-consolidates-the-mdc1-dependent-dna-double-strand-break-response-by-counteracting-the-sumo-targeted-ubiquitin-ligase-rnf4
#9
Annika Pfeiffer, Martijn S Luijsterburg, Klara Acs, Wouter W Wiegant, Angela Helfricht, Laura K Herzog, Melania Minoia, Claudia Böttcher, Florian A Salomons, Haico van Attikum, Nico P Dantuma
The SUMO-targeted ubiquitin ligase RNF4 functions at the crossroads of the SUMO and ubiquitin systems. Here, we report that the deubiquitylation enzyme (DUB) ataxin-3 counteracts RNF4 activity during the DNA double-strand break (DSB) response. We find that ataxin-3 negatively regulates ubiquitylation of the checkpoint mediator MDC1, a known RNF4 substrate. Loss of ataxin-3 markedly decreases the chromatin dwell time of MDC1 at DSBs, which can be fully reversed by co-depletion of RNF4. Ataxin-3 is recruited to DSBs in a SUMOylation-dependent fashion, and in vitro it directly interacts with and is stimulated by recombinant SUMO, defining a SUMO-dependent mechanism for DUB activity toward MDC1...
March 8, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28273895/the-dynamic-interacting-landscape-of-mapl-reveals-essential-functions-for-sumoylation-in-innate-immunity
#10
Karine Doiron, Vanessa Goyon, Etienne Coyaud, Sanjeeva Rajapakse, Brian Raught, Heidi M McBride
Activation of the innate immune response triggered by dsRNA viruses occurs through the assembly of the Mitochondrial Anti-Viral Signaling (MAVS) complex. Upon recognition of viral dsRNA, the cytosolic receptor RIG-I is activated and recruited to MAVS to activate the immune signaling response. We here demonstrate a strict requirement for a mitochondrial anchored protein ligase, MAPL (also called MUL1) in the signaling events that drive the transcriptional activation of antiviral genes downstream of Sendai virus infection, both in vivo and in vitro...
December 2017: Scientific Reports
https://www.readbyqxmd.com/read/28272518/sumoylation-stabilizes-rack1b-and-enhance-its-interaction-with-rap2-6-in-the-abscisic-acid-response
#11
Rongkai Guo, Weining Sun
The highly conserved eukaryotic WD40 repeat protein, Receptor for Activated C Kinase 1 (RACK1), is involved in the abscisic acid (ABA) response in Arabidopsis. However, the regulation of RACK1 and the proteins with which it interacts are poorly understood. Here, we show that RACK1B is sumoylated at four residues, Lys50, Lys276, Lys281 and Lys291. Sumoylation increases RACK1B stability and its tolerance to ubiquitination-mediated degradation in ABA response. As a result, sumoylation leads to enhanced interaction between RACK1B and RAP2...
March 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28267405/genetic-characterization-of-t-dna-insertions-in-the-genome-of-the-arabidopsis-thaliana-sumo1-2-knock-down-line
#12
Valentin Hammoudi, Georgios Vlachakis, Ronnie de Jonge, Timo M Breit, Harrold A van den Burg
Sumoylation is an essential post-translational modification in Arabidopsis thaliana, which entails the conjugation of the SUMO protein onto lysine residues in target proteins. In Arabidopsis, 2 closely related genes, SUMO1 and SUMO2, act redundantly and are in combination essential for plant development, i.e. the combined loss of SUMO1 and SUMO2 results in embryo-lethality. To circumvent this lethality, SUMO2 was previously knocked down in a sumo1 knockout background by expressing an artificial microRNA that targets SUMO2 (amiR-SUMO2)...
March 4, 2017: Plant Signaling & Behavior
https://www.readbyqxmd.com/read/28265077/arsenic-trioxide-targets-mthfd1-and-sumo-dependent-nuclear-de-novo-thymidylate-biosynthesis
#13
Elena Kamynina, Erica R Lachenauer, Aislyn C DiRisio, Rebecca P Liebenthal, Martha S Field, Patrick J Stover
Arsenic exposure increases risk for cancers and is teratogenic in animal models. Here we demonstrate that small ubiquitin-like modifier (SUMO)- and folate-dependent nuclear de novo thymidylate (dTMP) biosynthesis is a sensitive target of arsenic trioxide (As2O3), leading to uracil misincorporation into DNA and genome instability. Methylenetetrahydrofolate dehydrogenase 1 (MTHFD1) and serine hydroxymethyltransferase (SHMT) generate 5,10-methylenetetrahydrofolate for de novo dTMP biosynthesis and translocate to the nucleus during S-phase, where they form a multienzyme complex with thymidylate synthase (TYMS) and dihydrofolate reductase (DHFR), as well as the components of the DNA replication machinery...
March 6, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28262828/senp3-mediated-desumoylation-of-drp1-facilitates-interaction-with-mff-to-promote-cell-death
#14
Chun Guo, Kevin A Wilkinson, Ashley J Evans, Philip P Rubin, Jeremy M Henley
The GTPase dynamin-related protein 1 (Drp1) is essential for physiological and pathophysiological mitochondrial fission. DeSUMOylation of Drp1 by the enzyme SENP3 promotes cell death during reperfusion after ischaemia by enhancing Drp1 partitioning to the mitochondrial outer membrane (MOM), which causes cytochrome c release and apoptosis. However, how deSUMOylation recruits Drp1 to the MOM is unknown. Here we show that deSUMOylation selectively promotes Drp1 binding to the MOM resident adaptor protein mitochondrial fission factor (Mff)...
March 6, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28254775/global-analysis-of-sumo-binding-proteins-identifies-sumoylation-as-a-key-regulator-of-the-ino80-chromatin-remodeling-complex
#15
Eric Cox, Woochang Hwang, Ijeoma Uzoma, Jianfei Hu, Catherine Guzzo, Junseop Jeong, Michael Matunis, Jiang Qian, Heng Zhu, Seth Blackshaw
SUMOylation is a critical regulator of a broad range of cellular processes, and is thought to do so in part by modulation of protein interaction. To comprehensively identify human proteins whose interaction is modulated by SUMOylation, we developed an in vitro binding assay using human proteome microarrays to identify targets of SUMO1 and SUMO2. We then integrated these results with protein SUMOylation and protein-protein interaction data to perform network motif analysis. We focused on a single network motif we termed a SUMOmodPPI (SUMO-modulated Protein-Protein Interaction) that included the INO80 chromatin remodeling complex subunits TFPT and INO80E...
March 2, 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28253371/autophagy-regulates-ubc9-levels-during-viral-mediated-tumorigenesis
#16
Domenico Mattoscio, Chiara Casadio, Claudia Miccolo, Fausto Maffini, Andrea Raimondi, Carlo Tacchetti, Tarik Gheit, Marta Tagliabue, Viviana E Galimberti, Francesca De Lorenzi, Michael Pawlita, Fausto Chiesa, Mohssen Ansarin, Massimo Tommasino, Susanna Chiocca
UBC9, the sole E2-conjugating enzyme required for SUMOylation, is a key regulator of essential cellular functions and, as such, is frequently altered in cancers. Along these lines, we recently reported that its expression gradually increases during early stages of human papillomavirus (HPV)-mediated cervical lesions transformation. However, a better understanding of how UBC9 is exploited by transforming viral oncoproteins is still needed. In the present study, we show that in human samples HPV drives UBC9 up-regulation also in very early steps of head and neck tumorigenesis, pointing to the important role for UBC9 in the HPV-mediated carcinogenic program...
March 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28250213/large-scale-purification-of-small-ubiquitin-like-modifier-sumo-modified-proteins-from-schizosaccharomyces-pombe
#17
Minghua Nie, Michael N Boddy
Covalent protein modification by sumoylation (i.e., addition of small ubiquitin-like modifiers [SUMOs]) regulates a broad spectrum of critical functions in eukaryotic cells; however, usually ≤1% of a given protein is modified as a result of the highly dynamic nature of sumoylation. As such, capturing and identifying sumoylated proteins are both important in biological studies and very challenging tasks. Here we report a tailored purification protocol that includes rapid and complete cell disruption, coupled to highly stringent isolation of sumoylated proteins...
March 1, 2017: Cold Spring Harbor Protocols
https://www.readbyqxmd.com/read/28250117/the-nd10-component-promyelocytic-leukemia-protein-acts-as-an-e3-ligase-for-sumoylation-of-the-major-immediate-early-protein-ie1-of-human-cytomegalovirus
#18
Nina Reuter, Eva-Maria Schilling, Myriam Scherer, Regina Müller, Thomas Stamminger
Previous studies identified the nuclear domain 10 (ND10) components PML, hDaxx, and Sp100 as factors of an intrinsic immune response against human cytomegalovirus (HCMV). This antiviral function of ND10, however, is antagonized by viral effector proteins like IE1p72, which induces a dispersal of ND10. Furthermore, we have shown that both major immediate-early proteins of HCMV, IE1p72 and IE2p86, transiently co-localize with ND10 subnuclear structures and undergo modification by the covalent attachment of SUMO...
March 1, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28250012/innate-immunity-to-rna-virus-is-regulated-by-temporal-and-reversible-sumoylation-of-rig-i-and-mda5
#19
Ming-Ming Hu, Chen-Yang Liao, Qing Yang, Xue-Qin Xie, Hong-Bing Shu
Sensing of viral RNA by the cytosolic receptors RIG-I and melanoma differentiation-associated gene 5 (MDA5) leads to innate antiviral response. How RIG-I and MDA5 are dynamically regulated in innate antiviral response is not well understood. Here, we show that TRIM38 positively regulates MDA5- and RIG-I-mediated induction of downstream genes and acts as a SUMO E3 ligase for their dynamic sumoylation at K43/K865 and K96/K888, respectively, before and after viral infection. The sumoylation of MDA5 and RIG-I suppresses their K48-linked polyubiquitination and degradation in uninfected or early-infected cells...
March 1, 2017: Journal of Experimental Medicine
https://www.readbyqxmd.com/read/28240261/nur77-suppresses-hepatocellular-carcinoma-via-switching-glucose-metabolism-toward-gluconeogenesis-through-attenuating-phosphoenolpyruvate-carboxykinase-sumoylation
#20
Xue-Li Bian, Hang-Zi Chen, Peng-Bo Yang, Ying-Ping Li, Fen-Na Zhang, Jia-Yuan Zhang, Wei-Jia Wang, Wen-Xiu Zhao, Sheng Zhang, Qi-Tao Chen, Yu Zheng, Xiao-Yu Sun, Xiao-Min Wang, Kun-Yi Chien, Qiao Wu
Gluconeogenesis, an essential metabolic process for hepatocytes, is downregulated in hepatocellular carcinoma (HCC). Here we show that the nuclear receptor Nur77 is a tumour suppressor for HCC that regulates gluconeogenesis. Low Nur77 expression in clinical HCC samples correlates with poor prognosis, and a Nur77 deficiency in mice promotes HCC development. Nur77 interacts with phosphoenolpyruvate carboxykinase (PEPCK1), the rate-limiting enzyme in gluconeogenesis, to increase gluconeogenesis and suppress glycolysis, resulting in ATP depletion and cell growth arrest...
February 27, 2017: Nature Communications
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