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https://www.readbyqxmd.com/read/28101176/anticancer-effects-of-valproic-acid-on-oral-squamous-cell-carcinoma-via-sumoylation-in-vivo-and-in-vitro
#1
Zhijian Sang, Yang Sun, Hong Ruan, Yong Cheng, Xiaojun Ding, Youcheng Yu
Aberrant histone deacetylase (HDAC) has a key role in the neoplastic process associated with the epigenetic patterns of tumor-related genes. The present study was performed to investigate the effects and determine the mechanism of action of the HDAC inhibitor, valproic acid (VPA), on the CAL27 cell line derived from oral squamous cell carcinoma (OSCC). The effects of VPA on the viability of CAL27 cells were investigated using MTT assays. Alterations in the cell cycle and apoptosis were also examined using propidium iodide (PI) and Annexin V-PI assays, and were subequently analyzed by flow cytometry...
December 2016: Experimental and Therapeutic Medicine
https://www.readbyqxmd.com/read/28098164/uncovering-the-sumoylation-and-ubiquitylation-crosstalk-in-human-cells-using-sequential-peptide-immunopurification
#2
Frédéric Lamoliatte, Francis P McManus, Ghizlane Maarifi, Mounira K Chelbi-Alix, Pierre Thibault
Crosstalk between the SUMO and ubiquitin pathways has recently been reported. However, no approach currently exists to determine the interrelationship between these modifications. Here, we report an optimized immunoaffinity method that permits the study of both protein ubiquitylation and SUMOylation from a single sample. This method enables the unprecedented identification of 10,388 SUMO sites in HEK293 cells. The sequential use of SUMO and ubiquitin remnant immunoaffinity purification facilitates the dynamic profiling of SUMOylated and ubiquitylated proteins in HEK293 cells treated with the proteasome inhibitor MG132...
January 18, 2017: Nature Communications
https://www.readbyqxmd.com/read/28096404/torc1-dependent-sumoylation-of-rpc82-promotes-rna-polymerase-iii-assembly-and-activity
#3
Pierre Chymkowitch, Aurélie Nguéa P, Håvard Aanes, Joseph Robertson, Arne Klungland, Jorrit M Enserink
Maintaining cellular homeostasis under changing nutrient conditions is essential for the growth and development of all organisms. The mechanisms that maintain homeostasis upon loss of nutrient supply are not well understood. By mapping the SUMO proteome in Saccharomyces cerevisiae, we discovered a specific set of differentially sumoylated proteins mainly involved in transcription. RNA polymerase III (RNAPIII) components, including Rpc53, Rpc82, and Ret1, are particularly prominent nutrient-dependent SUMO targets...
January 17, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28095500/senp7-potentiates-cgas-activation-by-relieving-sumo-mediated-inhibition-of-cytosolic-dna-sensing
#4
Ye Cui, Huansha Yu, Xin Zheng, Rui Peng, Qiang Wang, Yi Zhou, Rui Wang, Jiehua Wang, Bo Qu, Nan Shen, Qiang Guo, Xing Liu, Chen Wang
Cyclic GMP-AMP (cGAMP) synthase (cGAS, a.k.a. MB21D1), a cytosolic DNA sensor, catalyzes formation of the second messenger 2'3'-cGAMP that activates the stimulator of interferon genes (STING) signaling. How the cGAS activity is modulated remains largely unknown. Here, we demonstrate that sentrin/SUMO-specific protease 7 (SENP7) interacted with and potentiated cGAS activation. The small ubiquitin-like modifier (SUMO) was conjugated onto the lysine residues 335, 372 and 382 of cGAS, which suppressed its DNA-binding, oligomerization and nucleotidyl-transferase activities...
January 17, 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28088449/the-role-of-sumoylation-in-ageing-and-senescent-decline
#5
REVIEW
Andrea Princz, Nektarios Tavernarakis
Posttranslational protein modifications are playing crucial roles in essential cellular mechanisms. SUMOylation is a reversible posttranslational modification of specific target proteins by the attachment of a small ubiquitin-like protein. Although the mechanism of conjugation of SUMO to proteins is analogous to ubiquitination, it requires its own, specific set of enzymes. The consequences of SUMOylation are widely variable, depending on the physiological state of the cell and the attached SUMO isoform. Accumulating recent findings have revealed a prominent role of SUMOylation in molecular pathways that govern senescence and ageing...
January 11, 2017: Mechanisms of Ageing and Development
https://www.readbyqxmd.com/read/28074026/promyelocytic-leukemia-protein-pml-controls-listeria-monocytogenes-infection
#6
David Ribet, Valérie Lallemand-Breitenbach, Omar Ferhi, Marie-Anne Nahori, Hugo Varet, Hugues de Thé, Pascale Cossart
: The promyelocytic leukemia protein (PML) is the main organizer of stress-responsive subnuclear structures called PML nuclear bodies. These structures recruit multiple interactors and modulate their abundance or their posttranslational modifications, notably by the SUMO ubiquitin-like modifiers. The involvement of PML in antiviral responses is well established. In contrast, the role of PML in bacterial infection remains poorly characterized. Here, we show that PML restricts infection by the pathogenic bacterium Listeria monocytogenes but not by Salmonella enterica serovar Typhimurium...
January 10, 2017: MBio
https://www.readbyqxmd.com/read/28067168/sumoylation-in-neurological-diseases
#7
F-Y Liu, Y-F Liu, Y Yang, Z-W Luo, J-W Xiang, Z-G Chen, R-L Qi, T-H Yang, Y Xiao, W-J Qing, D W-C Li
Since the discovery of SUMOs (small ubiquitin-like modifiers) over 20 years ago, sumoylation has recently emerged as an important post-translational modification involved in almost all aspects of cellular physiology. In neurons, sumoylation dynamically modulates protein function and consequently plays an important role in neuronal maturation, synapse formation and plasticity. Thus, the dysfunction of sumoylation pathway is associated with many different neurological disorders. Hundreds of different proteins implicated in the pathogenesis of neurological disorders are SUMO-modified, indicating the importance of sumoylation involved in the neurological diseases...
January 9, 2017: Current Molecular Medicine
https://www.readbyqxmd.com/read/28059716/a-sumo-ubiquitin-relay-recruits-proteasomes-to-chromosome-axes-to-regulate-meiotic-recombination
#8
H B D Prasada Rao, Huanyu Qiao, Shubhang K Bhatt, Logan R J Bailey, Hung D Tran, Sarah L Bourne, Wendy Qiu, Anusha Deshpande, Ajay N Sharma, Connor J Beebout, Roberto J Pezza, Neil Hunter
Meiosis produces haploid gametes through a succession of chromosomal events including pairing, synapsis and recombination. Mechanisms that orchestrate these events remain poorly understood. We found that the SUMO-modification and ubiquitin-proteasome systems regulate the major events of meiotic prophase in mouse. Interdependent localization of SUMO, ubiquitin and proteasomes along chromosome axes was mediated largely by RNF212 and HEI10, two E3 ligases that are also essential for crossover recombination. RNF212-dependent SUMO conjugation effected a checkpoint-like process that stalls recombination by rendering the turnover of a subset of recombination factors dependent on HEI10-mediated ubiquitylation...
January 5, 2017: Science
https://www.readbyqxmd.com/read/28039207/nup358-binds-to-ago-proteins-through-its-sumo-interacting-motifs-and-promotes-the-association-of-target-mrna-with-mirisc
#9
Manas Ranjan Sahoo, Swati Gaikwad, Deepak Khuperkar, Maitreyi Ashok, Mary Helen, Santosh Kumar Yadav, Aditi Singh, Indrasen Magre, Prachi Deshmukh, Supriya Dhanvijay, Pabitra Kumar Sahoo, Yogendra Ramtirtha, Mallur Srivatsan Madhusudhan, Pananghat Gayathri, Vasudevan Seshadri, Jomon Joseph
MicroRNA (miRNA)-guided mRNA repression, mediated by the miRNA-induced silencing complex (miRISC), is an important component of post-transcriptional gene silencing. However, how miRISC identifies the target mRNA in vivo is not well understood. Here, we show that the nucleoporin Nup358 plays an important role in this process. Nup358 localizes to the nuclear pore complex and to the cytoplasmic annulate lamellae (AL), and these structures dynamically associate with two mRNP granules: processing bodies (P bodies) and stress granules (SGs)...
December 30, 2016: EMBO Reports
https://www.readbyqxmd.com/read/28029095/sumoylation-of-nav1-2-channels-mediates-the-early-response-to-acute-hypoxia-in-central-neurons
#10
Leigh D Plant, Jeremy D Marks, Steven An Goldstein
The mechanism for the earliest response of central neurons to hypoxia-an increase in voltage-gated sodium current (INa)-has been unknown. Here, we show that hypoxia activates the Small Ubiquitin-like Modifier (SUMO) pathway in rat cerebellar granule neurons (CGN) and that SUMOylation of NaV1.2 channels increases INa. The time-course for SUMOylation of single NaV1.2 channels at the cell surface and changes in INa coincide, and both are prevented by mutation of NaV1.2-Lys38 or application of a deSUMOylating enzyme...
December 28, 2016: ELife
https://www.readbyqxmd.com/read/28017139/sumoylation-in-cellular-senescence-and-aging
#11
L Gong, Q Sun, D W-C Li
Sumoylation is a reversible post-translational modification that conjugates small peptide SUMO (small ubiquitin-like modifier) to a target protein. Global protein sumoylation and expression of components in sumoylation pathway were recently found to be altered in the process of organismal aging. In addition, key factors controlling cellular senescence are known to be sumoylated. This review will summarize current information on the function of sumoylation in cellular senescence and aging.
December 22, 2016: Current Molecular Medicine
https://www.readbyqxmd.com/read/28017138/sumoylation-pathway-as-potential-therapeutic-targets-in-cancer
#12
L Gong, R Qi, D W-C Li
Sumoylation is a covalent protein posttranslational modification that conjugates the small ubiquitin-like peptide SUMO to substrate. Sumoylation is critically implicated in multiple biological processes, including cell proliferation, differentiation, senescence and apoptosis, etc. Therefore, it is not surprising that dysregulation of sumoylation has been implicated in tumorigenesis and different types of cancer were found to be addicted to functional sumoylation pathway. The potential role for sumoylation as a therapeutic target in caner is emerging...
December 22, 2016: Current Molecular Medicine
https://www.readbyqxmd.com/read/28017135/role-of-sumoylation-in-heart-development-and-cardiovascular-diseases
#13
L Zhang, T-H Yang, D W-C Li
Heart is an extremely important organ, and cardiovascular disorders emerge as primary life-threatening disease in human life. Aberrant post-translational modifications (PTMs) on cardiac proteins are closely correlated with pathological abnormalities in heart. SUMOylation, one of the most prevalent PTMs with thousands of substrates throughout the cell including critical subcellular organelles, has been shown to precisely fine-tune the cell survival and proliferation during heart development, and delicately control the function of mitochondrion and sarcoplasmic reticulum in physiological heart functioning...
December 23, 2016: Current Molecular Medicine
https://www.readbyqxmd.com/read/28011904/multifunctional-roles-of-saccharomyces-cerevisiae-srs2-protein-in-replication-recombination-and-repair
#14
Hengyao Niu, Hannah L Klein
The Saccharomyces cerevisiae Srs2 DNA helicase has important roles in DNA replication, recombination and repair. In replication, Srs2 aids in repair of gaps by repair synthesis by preventing gaps from being used to initiate recombination. This is considered to be an anti-recombination role. In recombination, Srs2 plays both pro-recombination and anti-recombination roles to promote the synthesis-dependent strand annealing (SDSA) recombination pathway and to inhibit gaps from initiating homologous recombination (HR)...
December 23, 2016: FEMS Yeast Research
https://www.readbyqxmd.com/read/28000315/the-mechanism-of-p53-rescue-by-susp4
#15
Do-Hyoung Kim, Chewook Lee, Si-Hyung Lee, Kyung-Tae Kim, Joan J Han, Eun-Ji Cha, Ji-Eun Lim, Ye-Jin Cho, Seung-Hee Hong, Kyou-Hoon Han
p53 is an important tumor-suppressor protein deactivation of which by mdm2 results in cancers. A SUMO-specific protease 4 (SUSP4) was shown to rescue p53 from mdm2-mediated deactivation, but the mechanism is unknown. The discovery by NMR spectroscopy of a "p53 rescue motif" in SUSP4 that disrupts p53-mdm2 binding is presented. This 29-residue motif is pre-populated with two transient helices connected by a hydrophobic linker. The helix at the C-terminus binds to the well-known p53-binding pocket in mdm2 whereas the N-terminal helix serves as an affinity enhancer...
December 21, 2016: Angewandte Chemie
https://www.readbyqxmd.com/read/27995772/a-novel-tomato-sumo-e3-ligase-slsiz1-confers-drought-tolerance-in-transgenic-tobacco
#16
Song Zhang, Kunyang Zhuang, Shiju Wang, Jinlian Lv, Na'na Ma, Qingwei Meng
SUMOylation is an important post-translational modification process that regulates different cellular functions in eukaryotes. SIZ/PIAS-type SAP and Miz1 (SIZ1) proteins exhibit SUMO E3 ligase activity, which modulates SUMOylation. However, SIZ1 in tomato has been rarely investigated. In this study, a tomato SIZ1 gene (SlSIZ1) was isolated and its molecular characteristics and role in tolerance to drought stress were described. SlSIZ1 was up-regulated by cold, sodium chloride (NaCl), polyethylene glycol (PEG), hydrogen peroxide (H2 O2 ) and abscisic acid (ABA), and the corresponding proteins were localized in the nucleus...
December 20, 2016: Journal of Integrative Plant Biology
https://www.readbyqxmd.com/read/27994213/host-cell-nuclear-localization-of-shigella-flexneri-effector-ospf-is-facilitated-by-sumoylation
#17
Kyungmin Jo, Eun Jin Kim, Hyun Jin Yu, Cheol-Heui Yun, Dong Wook Kim
When Shigella infect host cells, various effecter molecules are delivered into cytoplasm of the host cell through the type III secretion system (TTSS) to facilitate their invasion process and control the host immune responses. Among these effectors, the S. flexneri effector OspF dephosphorylates mitogen-activated protein kinases (MAPK) and translocates itself to the nucleus, thus preventing histone H3 modification to regulate expression of pro-inflammatory cytokines. Despite the critical role of OspF, the mechanism by which OspF localizes in the nucleus has remained to be elucidated...
December 20, 2016: Journal of Microbiology and Biotechnology
https://www.readbyqxmd.com/read/27986376/bilateral-upregulation-of-%C3%AE-synuclein-expression-in-the-mouse-substantia-nigra-by-intracranial-rotenone-treatment
#18
Candace H Carriere, Na Hyea Kang, Lennard P Niles
The pesticide rotenone has been shown to cause systemic inhibition of mitochondrial complex I activity, with consequent degeneration of dopamine neurons along the nigrostriatal pathway, as observed in Parkinson's disease (PD). Recently, intracranial infusion of rotenone was found to increase the protein levels of the Lewy body constituents, α-synuclein and small ubiquitin-related modifier-1(SUMO-1), in the lesioned hemisphere of the mouse brain. These findings are supportive of a mouse model of PD, but information about the dopamine-synthesizing enzyme, tyrosine hydroxylase (TH), an essential marker of dopaminergic status, was not reported...
December 13, 2016: Experimental and Toxicologic Pathology: Official Journal of the Gesellschaft Für Toxikologische Pathologie
https://www.readbyqxmd.com/read/27960034/a-leukemogenic-kinase-fip1l1-pdgfra-and-a-sumo-e3-ligase-pias1-form-a-positive-crosstalk-via-their-enzymatic-activities
#19
Makoto Ibata, Junko Iwasaki, Yoichiro Fujioka, Koji Nakagawa, Stephanie Darmanin, Masahiro Onozawa, Daigo Hashimoto, Yusuke Ohba, Shigetsugu Hatakeyama, Takanori Teshima, Takeshi Kondo
Fusion tyrosine kinases play a crucial role in the development of hematological malignancies. FIP1L1-PDGFRA is a leukemogenic fusion kinase that causes chronic eosinophilic leukemia. As a constitutively active kinase, FIP1L1-PDGFRA stimulates downstream signaling molecules, leading to cellular proliferation and the generation of an anti-apoptotic state. Contribution of the N-terminal FIP1L1 portion is necessary for FIP1L1-PDGFRA to exert its full transforming activity, but the underlying mechanisms have not been fully characterized...
December 13, 2016: Cancer Science
https://www.readbyqxmd.com/read/27940916/hierarchical-crmp2-posttranslational-modifications-control-nav1-7-function
#20
Erik T Dustrude, Aubin Moutal, Xiaofang Yang, Yuying Wang, May Khanna, Rajesh Khanna
Voltage-gated sodium channels are crucial determinants of neuronal excitability and signaling. Trafficking of the voltage-gated sodium channel NaV1.7 is dysregulated in neuropathic pain. We identify a trafficking program for NaV1.7 driven by hierarchical interactions with posttranslationally modified versions of the binding partner collapsin response mediator protein 2 (CRMP2). The binding described between CRMP2 and NaV1.7 was enhanced by conjugation of CRMP2 with small ubiquitin-like modifier (SUMO) and further controlled by the phosphorylation status of CRMP2...
December 27, 2016: Proceedings of the National Academy of Sciences of the United States of America
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