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SUMOylation

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https://www.readbyqxmd.com/read/29051266/sumoylation-of-human-septins-is-critical-for-septin-filament-bundling-and-cytokinesis
#1
David Ribet, Serena Boscaini, Clothilde Cauvin, Martin Siguier, Serge Mostowy, Arnaud Echard, Pascale Cossart
Septins are cytoskeletal proteins that assemble into nonpolar filaments. They are critical in diverse cellular functions, acting as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization. Human septins are encoded by 13 different genes and are classified into four groups based on sequence homology (SEPT2, SEPT3, SEPT6, and SEPT7 groups). In yeast, septins were among the first proteins reported to be modified by SUMOylation, a ubiquitin-like posttranslational modification...
October 19, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/29050267/reversible-regulation-of-orc2-sumoylation-by-pias4-and-senp2
#2
Ronghua Wang, Fangming Liu, Yongxu Zhao, Dan Wu, Lihan Chen, Edward T H Yeh, Chao Huang
The small ubiquitin-related modifier (SUMO) system is essential for smooth progression of cell cycle at the G2/M phase. Many centromeric proteins are reversibly SUMOylated to ensure proper chromosome segregation at the mitosis. SUMOylation of centromeric Origin Recognition Complex subunit 2 (ORC2) at the G2/M phase is essential in maintaining genome integrity. However, how ORC2 SUMOylation is regulated remains largely unclear. Here we show that ORC2 SUMOylation is reversibly controlled by SUMO E3 ligase PIAS4 and De-SUMOylase SENP2...
September 19, 2017: Oncotarget
https://www.readbyqxmd.com/read/29048423/identification-of-cross-talk-between-sumoylation-and-ubiquitylation-using-a-sequential-peptide-immunopurification-approach
#3
Francis P McManus, Frédéric Lamoliatte, Pierre Thibault
Ubiquitin and ubiquitin-like modifiers (UBLs) such as small ubiquitin-like modifier (SUMO) can act as antagonists to one another by competing to occupy similar residues in the proteome. In addition, SUMO and ubiquitin can be coupled to each other at key lysine residues to form highly branched protein networks. The interplay between these modifications governs important biological processes such as double-strand break repair and meiotic recombination. We recently developed an approach that permits the identification of proteins that are modified by both SUMOylation and ubiquitylation...
November 2017: Nature Protocols
https://www.readbyqxmd.com/read/29045470/structural-and-functional-analysis-of-smo-1-the-sumo-homolog-in-caenorhabditis-elegans
#4
Parag Surana, Chandrakala M Gowda, Vasvi Tripathi, Limor Broday, Ranabir Das
SUMO proteins are important post-translational modifiers involved in multiple cellular pathways in eukaryotes, especially during the different developmental stages in multicellular organisms. The nematode C. elegans is a well known model system for studying metazoan development and has a single SUMO homolog, SMO-1. Interestingly, SMO-1 modification is linked to embryogenesis and development in the nematode. However, high-resolution information about SMO-1 and the mechanism of its conjugation is lacking. In this work, we report the high-resolution three dimensional structure of SMO-1 solved by NMR spectroscopy...
2017: PloS One
https://www.readbyqxmd.com/read/29045383/drug-discovery-controlling-protein-sumoylation
#5
John S Schneekloth
No abstract text is available yet for this article.
October 18, 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/29039464/hypothermia-inhibits-the-proliferation-of-bone-marrow-derived-mesenchymal-stem-cells-and-increases-tolerance-to-hypoxia-by-enhancing-sumoylation
#6
Xiaozhi Liu, Wenbo Ren, Zhongmin Jiang, Zhiguo Su, Xiaofang Ma, Yanxia Li, Rongcai Jiang, Jianning Zhang, Xinyu Yang
Hypothermia therapy has a positive effect on patients with severe brain injury. Recent studies have shown that mild hypothermia increases the survival of bone marrow-derived mesenchymal stem cells (BMSCs) in a hypoxic environment; however, the underlying mechanisms are not yet fully understood. Small ubiquitin-like modifiers (SUMOs) are sensitive to temperature stress reactions and are considered to exert a protective effect. In this study, we examined the protective effects of hypothermia on BMSCs in terms of SUMO protein modification...
September 29, 2017: International Journal of Molecular Medicine
https://www.readbyqxmd.com/read/29038616/sumo-e3-ligase-piasy-mediates-high-glucose-induced-activation-of-nf-%C3%AE%C2%BAb-inflammatory-signaling-in-rat-mesangial-cells
#7
Wei Huang, Yaling Liang, Jianhua Dong, Luping Zhou, Chenlin Gao, Chunxia Jiang, Meijuan Chen, Yang Long, Yong Xu
BACKGROUND: Sumoylation is extensively involved in the regulation of NF-κB signaling. PIASy, as a SUMO E3 ligase, has been proved to mediate sumoylation of IκB kinase γ (IKKγ) and contribute to the activation of NF-κB under genotoxic agent stimulation. However, the association of PIASy and NF-κB signaling in the pathogenesis of diabetic nephropathy (DN) has not been defined. METHODS: Rat glomerular mesangial cells (GMCs) were stimulated by high glucose; siRNA was constructed to silence the expression of PIASy; the expression of PIASy, SUMO isoforms (SUMO1, SUMO2/3), and NF-κB signaling components was analyzed by Western blot; the interaction between IKKγ and SUMO proteins was detected by coimmunoprecipitation; and the release of inflammatory cytokines MCP-1 and IL-6 was assayed by ELISA...
2017: Mediators of Inflammation
https://www.readbyqxmd.com/read/29036198/the-homeodomain-interacting-protein-kinase-hpk-1-preserves-protein-homeostasis-and-longevity-through-master-regulatory-control-of-the-hsf-1-chaperone-network-and-torc1-restricted-autophagy-in-caenorhabditis-elegans
#8
Ritika Das, Justine A Melo, Manjunatha Thondamal, Elizabeth A Morton, Adam B Cornwell, Beresford Crick, Joung Heon Kim, Elliot W Swartz, Todd Lamitina, Peter M Douglas, Andrew V Samuelson
An extensive proteostatic network comprised of molecular chaperones and protein clearance mechanisms functions collectively to preserve the integrity and resiliency of the proteome. The efficacy of this network deteriorates during aging, coinciding with many clinical manifestations, including protein aggregation diseases of the nervous system. A decline in proteostasis can be delayed through the activation of cytoprotective transcriptional responses, which are sensitive to environmental stress and internal metabolic and physiological cues...
October 16, 2017: PLoS Genetics
https://www.readbyqxmd.com/read/29024335/fifty-shades-of-sumo-its-role-in-immunity-and-at-the-fulcrum-of-growth-defense-balance
#9
Vivek Verma, Fenella Crolley, Ari Sadanandom
The sessile nature of plants requires them to cope with an ever changing environment. Effective adaptive responses require sophisticated cellular mechanisms at post-transcriptional and -translational levels. Post-translational modification by Small Ubiquitin-like Modifier (SUMO) proteins is emerging as a key player in these adaptive responses. SUMO conjugation can rapidly change the overall fate of target proteins by altering their stability or interaction with partner proteins or DNA. SUMOylation entails an enzyme cascade that leads to the activation, conjugation and ligation of SUMO to lysine residues of target proteins...
October 10, 2017: Molecular Plant Pathology
https://www.readbyqxmd.com/read/29024118/rice-sumo-protease-overly-tolerant-to-salt-1-targets-the-transcription-factor-osbzip23-to-promote-drought-tolerance-in-rice
#10
Anjil Kumar Srivastava, Cunjin Zhang, Robert S Caine, Julie Gray, Ari Sadanandom
Conjugation of SUMO (Small Ubiquitin-like Modifier) protein to cellular targets is emerging as a very influential protein modification system. Once covalently bound SUMO conjugation can change the stability or functionality of its cognate target proteins. SUMO protease can rapidly reverse SUMO conjugation making this modification system highly dynamic. A major factor in the variation of SUMO-target function is the balance between the conjugated/de-conjugated forms. The mechanistic role of these regulatory SUMO proteases in mediating stress responses has not been defined in any crops...
October 10, 2017: Plant Journal: for Cell and Molecular Biology
https://www.readbyqxmd.com/read/29022905/c-abl-mediated-drp1-phosphorylation-promotes-oxidative-stress-induced-mitochondrial-fragmentation-and-neuronal-cell-death
#11
Lujun Zhou, Qiang Zhang, Peng Zhang, Lei Sun, Can Peng, Zengqiang Yuan, Jinbo Cheng
Oxidative stress-induced mitochondrial dysfunction and neuronal cell death have important roles in the development of neurodegenerative diseases. Dynamin related protein 1 (Drp1) is a critical factor in regulating mitochondrial dynamics. A variety of posttranslational modifications of Drp1 have been reported, including phosphorylation, ubiquitination, sumoylation and S-nitrosylation. In this study, we found that c-Abl phosphorylated Drp1 at tyrosine 266, 368 and 449 in vitro and in vivo, which augmented the GTPase activity of Drp1 and promoted Drp1-mediated mitochondrial fragmentation...
October 12, 2017: Cell Death & Disease
https://www.readbyqxmd.com/read/29021238/asy2-mer2-an-evolutionarily-conserved-mediator-of-meiotic-recombination-pairing-and-global-chromosome-compaction
#12
Sophie Tessé, Henri-Marc Bourbon, Robert Debuchy, Karine Budin, Emeline Dubois, Zhang Liangran, Romain Antoine, Tristan Piolot, Nancy Kleckner, Denise Zickler, Eric Espagne
Meiosis is the cellular program by which a diploid cell gives rise to haploid gametes for sexual reproduction. Meiotic progression depends on tight physical and functional coupling of recombination steps at the DNA level with specific organizational features of meiotic-prophase chromosomes. The present study reveals that every step of this coupling is mediated by a single molecule: Asy2/Mer2. We show that Mer2, identified so far only in budding and fission yeasts, is in fact evolutionarily conserved from fungi (Mer2/Rec15/Asy2/Bad42) to plants (PRD3/PAIR1) and mammals (IHO1)...
October 11, 2017: Genes & Development
https://www.readbyqxmd.com/read/29021212/protein-sumoylation-modification-and-its-associations-with-disease
#13
REVIEW
Yanfang Yang, Yu He, Xixi Wang, Ziwei Liang, Gu He, Peng Zhang, Hongxia Zhu, Ningzhi Xu, Shufang Liang
SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site...
October 2017: Open Biology
https://www.readbyqxmd.com/read/29020972/sumo1-modification-of-khsrp-regulates-tumorigenesis-by-preventing-the-tl-g-rich-mirna-biogenesis
#14
Haihua Yuan, Rong Deng, Xian Zhao, Ran Chen, Guofang Hou, Hailong Zhang, Yanli Wang, Ming Xu, Bin Jiang, Jianxiu Yu
BACKGROUND: MicroRNAs (miRNAs) are important regulators involved in diverse physiological and pathological processes including cancer. SUMO (small ubiquitin-like modifier) is a reversible protein modifier. We recently found that SUMOylation of TARBP2 and DGCR8 is involved in the regulation of the miRNA pathway. KHSRP is a single stranded nucleic acid binding protein with roles in transcription and mRNA decay, and it is also a component of the Drosha-DGCR8 complex promoting the miRNA biogenesis...
October 11, 2017: Molecular Cancer
https://www.readbyqxmd.com/read/29020638/proteomics-reveals-global-regulation-of-protein-sumoylation-by-atm-and-atr-kinases-during-replication-stress
#15
Stephanie Munk, Jón Otti Sigurðsson, Zhenyu Xiao, Tanveer Singh Batth, Giulia Franciosa, Louise von Stechow, Andres Joaquin Lopez-Contreras, Alfred Cornelis Otto Vertegaal, Jesper Velgaard Olsen
The mechanisms that protect eukaryotic DNA during the cumbersome task of replication depend on the precise coordination of several post-translational modification (PTM)-based signaling networks. Phosphorylation is a well-known regulator of the replication stress response, and recently an essential role for SUMOs (small ubiquitin-like modifiers) has also been established. Here, we investigate the global interplay between phosphorylation and SUMOylation in response to replication stress. Using SUMO and phosphoproteomic technologies, we identify thousands of regulated modification sites...
October 10, 2017: Cell Reports
https://www.readbyqxmd.com/read/29018572/enhanced-hoxa10-sumoylation-inhibits-embryo-implantation-in-women-with-recurrent-implantation-failure
#16
Ruiwei Jiang, Lijun Ding, Jianjun Zhou, Chenyang Huang, Qun Zhang, Yue Jiang, Jingyu Liu, Qiang Yan, Xin Zhen, Jianxin Sun, Guijun Yan, Haixiang Sun
HOXA10 has emerged as an important molecular marker of endometrial receptivity. Recurrent implantation failure (RIF) after in vitro fertilization-embryo transplantation (IVF-ET) treatment is associated with impaired endometrial receptivity, but the exact underlying mechanism of this phenomenon remains elusive. Here we found that HOXA10 was modified by small ubiquitin like-modifier 1 (SUMO1) at the evolutionarily conserved lysine 164 residue. Sumoylation inhibited HOXA10 protein stability and transcriptional activity without affecting its subcellular localization...
2017: Cell Death Discovery
https://www.readbyqxmd.com/read/28990926/irak2-directs-stimulus-dependent-nuclear-export-of-inflammatory-mrnas
#17
Hao Zhou, Katarzyna Bulek, Xiao Li, Tomasz Herjan, Minjia Yu, Wen Qian, Han Wang, Gao Zhou, Xing Chen, Hui Yang, Lingzi Hong, Junjie Zhao, Luke Qin, Koichi Fukuda, Annette Flotho, Ji Gao, Ashok Dongre, Julie A Carman, Zizhen Kang, Bing Su, Timothy S Kern, Jonathan D Smith, Thomas A Hamilton, Frauke Melchior, Paul L Fox, Xiaoxia Li
Expression of inflammatory genes is determined in part by post-transcriptional regulation of mRNA metabolism but how stimulus- and transcript-dependent nuclear export influence is poorly understood. Here we report a novel pathway in which LPS/TLR4 engagement promotes nuclear localization of IRAK2 to facilitate nuclear export of a specific subset of inflammation related mRNAs for translation in murine macrophages. IRAK2 kinase activity is required for LPS-induced RanBP2-mediated IRAK2 sumoylation and subsequent nuclear translocation...
October 9, 2017: ELife
https://www.readbyqxmd.com/read/28987385/sumoylation-of-iqgap1-promotes-the-development-of-colorectal-cancer
#18
Ziwei Liang, Yanfang Yang, Yu He, Pengbo Yang, Xixi Wang, Gu He, Peng Zhang, Hongxia Zhu, Ningzhi Xu, Xia Zhao, Shufang Liang
IQGAP1 is a conserved multifunctional protein implicated in tumorigenesis. An aberrant expression of IQGAP1 widely exists in many cancers, but the SUMOylation modification of IQGAP1 in carcinogenesis is unknown by now. Here we first time explore biological functions of IQGAP1 SUMOylation in promoting colorectal cancer progression in vitro and in vivo. The expression of IQGAP1 and its SUMOylation level are both increased in human colorectal carcinoma (CRC) cells and tissues. IQGAP1 is mainly SUMOylated by SUMO1 at the K1445 residue, which could stabilize IQGAP1 by reducing protein ubiquitination...
October 5, 2017: Cancer Letters
https://www.readbyqxmd.com/read/28981631/uv-radiation-induced-sumoylation-of-ddb2-regulates-nucleotide-excision-repair
#19
Chunhua Han, Ran Zhao, John Kroger, Jinshan He, Gulzar Wani, Qi-En Wang, Altaf A Wani
Subunit 2 of DNA damage-binding protein complex (DDB2) is an early sensor of nucleotide excision repair (NER) pathway for eliminating DNA damage induced by UV radiation (UVR) and cisplatin treatments of mammalian cells. DDB2 is modified by ubiquitin and poly(ADP-ribose) (PAR) in response to UVR, and these modifications play a crucial role in regulating NER. Here, using immuno-analysis of irradiated cell extracts, we have identified multiple post-irradiation modifications of DDB2 protein. Interestingly, although the DNA lesions induced by both UVR and cisplatin are corrected by NER, only the UV irradiation, but not the cisplatin treatment, induces any discernable DDB2 modifications...
July 22, 2017: Carcinogenesis
https://www.readbyqxmd.com/read/28979848/post-translational-modifications-of-arabidopsis-e3-sumo-ligase-atsiz1-are-controlled-by-environmental-conditions
#20
Joo Yong Kim, Jong Tae Song, Hak Soo Seo
Sumoylation regulates numerous cellular functions in plants as well as in other eukaryotic systems. However, the regulatory mechanisms controlling E3 small ubiquitin-related modifier (SUMO) ligase are not well understood. Here, post-translational modification of the Arabidopsis E3 SUMO ligase AtSIZ1 was shown to be specifically controlled by abiotic stresses. AtSIZ1 ubiquitination was induced by exposure to heat stress in transgenic plants overexpressing the E3 ubiquitin ligase COP1. In addition, AtSIZ1 ubiquitination was strongly enhanced in transgenic plants overexpressing SUMO isopeptidase ESD4 under heat stress...
October 2017: FEBS Open Bio
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