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Fengxi Meng, Xiaofeng Li, Hui Ren, Jiang Qian
The post-translational modifications of proteins are critical for the proper regulation of intracellular signal transduction. Among these modifications, small ubiquitin-related modifier (SUMO) is a ubiquitin-like protein that is covalently attached to the lysine residues of a variety of target proteins to regulate cellular processes, such as gene transcription, DNA repair, protein interaction and degradation, subcellular transport, and signal transduction. The most common approach to detecting protein SUMOylation is based on the expression and purification of recombinant tagged proteins in bacteria, allowing for an in vitro biochemical reaction which is simple and suitable for addressing mechanistic questions...
November 2, 2017: Journal of Visualized Experiments: JoVE
Ranja Sarkar
SUMO (small ubiquitin-like modifier) proteins interact with a large number of target proteins via a key regulatory event called sumoylation that encompasses activation, conjugation and ligation of SUMO proteins through specific E1, E2, and E3-type enzymes respectively. Single-molecule atomic force microscopic (AFM) experiments performed to unravel bound SUMO1 along its N-C termini direction reveal that E3-ligases (in the form of small peptides) increase mechanical stability (along the axis) of the flexible protein upon binding...
November 16, 2017: Mathematical Biosciences
Duncan J Clarke, Yoshiaki Azuma
DNA Topoisomerase IIα (Topo IIα) is a ubiquitous enzyme in eukaryotes that performs the strand passage reaction where a double helix of DNA is passed through a second double helix. This unique reaction is critical for numerous cellular processes. However, the enzyme also possesses a C-terminal domain (CTD) that is largely dispensable for the strand passage reaction but is nevertheless important for the fidelity of cell division. Recent studies have expanded our understanding of the roles of the Topo IIα CTD, in particular in mitotic mechanisms where the CTD is modified by Small Ubiquitin-like Modifier (SUMO), which in turn provides binding sites for key regulators of mitosis...
November 17, 2017: International Journal of Molecular Sciences
Joshua D Bernstock, Wei Yang, Daniel G Ye, Yuntian Shen, Stefano Pluchino, Yang-Ja Lee, John M Hallenbeck, Wulf Paschen
Post-translational protein modification by small ubiquitin-like modifier (SUMO) regulates a myriad of homeostatic and stress responses. The SUMOylation pathway has been extensively studied in brain ischemia. Convincing evidence is now at hand to support the notion that a major increase in levels of SUMOylated proteins is capable of inducing tolerance to ischemic stress. Therefore, the SUMOylation pathway has emerged as a promising therapeutic target for neuroprotection in the face of brain ischemia. Despite this, it is prudent to acknowledge that there are many key questions still to be addressed in brain ischemia related to SUMOylation...
January 1, 2017: Journal of Cerebral Blood Flow and Metabolism
Joshua D Bernstock, Daniel Ye, Jayden A Smith, Yang-Ja Lee, Florian A Gessler, Adam Yasgar, Jennifer Kouznetsova, Ajit Jadhav, Zhuoran Wang, Stefano Pluchino, Wei Zheng, Anton Simeonov, John M Hallenbeck, Wei Yang
The development of novel neuroprotective treatments for acute stroke has been fraught with failures, which supports the view of ischemic brain damage as a highly complex multifactorial process. Post-translational modifications such as small ubiquitin-like modifier (SUMO)ylation have emerged as critical molecular regulatory mechanisms in states of both homeostasis and ischemic stress, as evidenced by our previous work. Accordingly, the clinical significance of the selective control of the global SUMOylation process has become apparent in studies of ischemic pathobiology and pathophysiology...
November 16, 2017: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
David J Hughes, Christian Tiede, Natalie Penswick, Anna Ah-San Tang, Chi H Trinh, Upasana Mandal, Katarzyna Z Zajac, Thembaninskosi Gaule, Gareth Howell, Thomas A Edwards, Jianxin Duan, Eric Feyfant, Michael J McPherson, Darren C Tomlinson, Adrian Whitehouse
Because protein-protein interactions underpin most biological processes, developing tools that target them to understand their function or to inform the development of therapeutics is an important task. SUMOylation is the posttranslational covalent attachment of proteins in the SUMO family (SUMO-1, SUMO-2, or SUMO-3), and it regulates numerous cellular pathways. SUMOylated proteins are recognized by proteins with SUMO-interaction motifs (SIMs) that facilitate noncovalent interactions with SUMO. We describe the use of the Affimer system of peptide display for the rapid isolation of synthetic binding proteins that inhibit SUMO-dependent protein-protein interactions mediated by SIMs both in vitro and in cells...
November 14, 2017: Science Signaling
Konstantin Tomanov, Lilian Nehlin, Ionida Ziba, Andreas Bachmair
The SUMO conjugation apparatus usually attaches single SUMO moieties to its substrates, but SUMO chains have also been identified. In order to better define biochemical requirements and characteristics of SUMO chain formation, mutations in surface-exposed Lys residues of Arabidopsis SUMO conjugating enzyme (SCE) were tested for in vitro activity. Lys to Arg changes in the amino-terminal region of SCE allowed SUMO acceptance from SUMO activating enzyme and supported substrate mono-sumoylation, but these mutations had significant effects on SUMO chain assembly...
November 13, 2017: Biochemical Journal
Ajay Goel
No abstract text is available yet for this article.
November 9, 2017: British Journal of Cancer
Lisa J Kost, Henning D Mootz
The small ubiquitin-like modifier (SUMO) can be assembled into polymeric chains as part of its diverse biochemical signal pattern when conjugated to substrate proteins. SUMO chain recognition is facilitated by receptor proteins containing at least two SUMO-interacting motifs (SIMs). Only little is known about the structure of SUMO chains, both in unliganded form and when complexed with multi-SIM protein partners. We have developed a FRET sensor based on a linear dimer of human SUMO-2 as a minimal SUMO chain analog...
November 9, 2017: Chembiochem: a European Journal of Chemical Biology
Fengmei Tan, Wenbin Dong, Xiaoping Lei, Xingling Liu, Qingping Li, Lan Kang, Shuai Zhao, Chan Zhang
A prospective study was performed to investigate the effects of hyperoxia on the expression of small ubiquitin‑related modifier (SUMO) and sirtuin 1 (SIRT1) proteins, and to examine interactions between these proteins in premature neonates with bronchopulmonary dysplasia (BPD). Peripheral blood mononuclear cells (PBMCs) were isolated from residual venous blood samples of 20 premature infants with BPD and 20 gender‑matched premature infants without BPD (non‑BPD group). Expression levels of SUMO and SIRT1 proteins in PBMCs were assessed by western blot analysis, and their interactions in PBMCs were detected using the immunoprecipitation assay...
November 8, 2017: Molecular Medicine Reports
Yanjun Zhou, Chunmei Ji, Mengda Cao, Miao Guo, Wen Huang, Weiwei Ni, Ling Meng, Haiwei Yang, Ji-Fu Wei
Small ubiquitin‑related modifier (SUMO) proteins bind to the lysine residue of target proteins to produce functionally mature proteins. The abnormal SUMOylation of certain target proteins is associated with diseases including cancer, heart disease, diabetes, arthritis, degenerative diseases and brain ischemia/stroke. Thus, there has been growing appreciation for the potential importance of the SUMO conjugation pathway as a target for treating these diseases. This review introduces the important steps in the reversible SUMOylation pathway...
November 1, 2017: International Journal of Molecular Medicine
Narayana Komaravelli, Maria Ansar, Roberto P Garofalo, Antonella Casola
Respiratory syncytial virus (RSV) is the most important cause of viral acute respiratory tract infections and hospitalizations in children, for which no vaccine or specific treatments are available. RSV causes airway mucosa inflammation and cellular oxidative damage by triggering production of reactive oxygen species and by inhibiting at the same time expression of antioxidant enzymes, via degradation of the transcription factor NF-E2-related factor 2 (NRF2). RSV infection induces NRF2 deacetylation, ubiquitination, and degradation through a proteasome-dependent pathway...
October 28, 2017: Free Radical Biology & Medicine
Manish Thiruvalluvan, Paul G Barghouth, Assaf Tsur, Limor Broday, Néstor J Oviedo
Mechanisms underlying anteroposterior body axis differences during adult tissue maintenance and regeneration are poorly understood. Here, we identify that post-translational modifications through the SUMO (Small Ubiquitin-like Modifier) machinery are evolutionarily conserved in the Lophotrocozoan Schmidtea mediterranea. Disruption of SUMOylation in adult animals by RNA-interference of the only SUMO E2 conjugating enzyme Ubc9 leads to a systemic increase in DNA damage and a remarkable regional defect characterized by increased cell death and loss of the posterior half of the body...
November 2, 2017: Cellular and Molecular Life Sciences: CMLS
Atsuhiko Fukuto, Masae Ikura, Tsuyoshi Ikura, Jiying Sun, Yasunori Horikoshi, Hiroki Shima, Kazuhiko Igarashi, Masayuki Kusakabe, Masahiko Harata, Naoki Horikoshi, Hitoshi Kurumizaka, Yoshiaki Kiuchi, Satoshi Tashiro
Histone exchange and histone post-translational modifications play important roles in the regulation of DNA metabolism, by re-organizing the chromatin configuration. We previously demonstrated that the histone variant H2A.Z-2 is rapidly exchanged at damaged sites after DNA double strand break induction in human cells. In yeast, the small ubiquitin-like modifier (SUMO) modification of H2A.Z is involved in the DNA damage response. However, whether the SUMO modification regulates the exchange of human H2A.Z-2 at DNA damage sites remains unclear...
November 2, 2017: Nucleus
Miguel Esteras, I-Chun Liu, Ambrosius P Snijders, Adam Jarmuz, Luis Aragon
Post-translational modification by the small ubiquitin-like modifier (SUMO) is an important mechanism regulating protein function. Identification of SUMO conjugation sites on substrates is a challenging task. Here we employed a proteomic method to map SUMO acceptor lysines in budding yeast proteins. We report the identification of 257 lysine residues where SUMO is potentially attached. Amongst the hits, we identified already known SUMO substrates and sites, confirming the success of the approach. In addition, we tested several of the novel substrates using SUMO immunoprecipitation analysis and confirmed that the SUMO acceptor lysines identified in these proteins are indeed bona fide SUMOylation sites...
October 2, 2017: Microbial Cell
Ryan J Lumpkin, Hongbo Gu, Yiying Zhu, Marilyn Leonard, Alla S Ahmad, Karl R Clauser, Jesse G Meyer, Eric J Bennett, Elizabeth A Komives
Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins. Proteome-wide detection of SUMOylation sites on target proteins typically requires ectopic expression of mutant SUMOs with introduced tryptic sites. Here, we report a method for proteome-wide, site-level detection of endogenous SUMOylation that uses α-lytic protease, WaLP...
October 27, 2017: Nature Communications
Shuhuan Fang, Honghai Hong, Lei Li, Dan He, Zumin Xu, Shaoyuan Zuo, Jing Han, Qiyuan Wu, Zhiyu Dai, Weibin Cai, Jianxing Ma, Chunkui Shao, Guoquan Gao, Xia Yang
Inhibition of tumour angiogenesis has an important role in antitumour therapy. However, a recent study indicates that antiangiogenesis therapy may lead to glucose-related protein 78 (GRP78) associated antiapoptotic resistance. The present study aims to elucidate the dual effects of plasminogen kringle 5 (K5) on tumour angiogenesis and apoptosis induction by targeting hypoxia-inducible factor 1α (HIF-1α) and GRP78. Co-immunoprecipitation and western blotting were used for examining the ubiquitination of HIF-1α and analysing angiogenesis and apoptosis-associated proteins...
October 26, 2017: Cell Death & Disease
Carlos F de la Cruz-Herrera, Maite Baz-Martínez, Ahmed El Motiam, Santiago Vidal, Manuel Collado, Anxo Vidal, Manuel S Rodríguez, Mariano Esteban, Carmen Rivas
Activated dsRNA-dependent serine/threonine kinase PKR phosphorylates the alpha subunit of eukaryotic initiation factor 2 (eIF2α), resulting in a shut-off of general translation, induction of apoptosis, and inhibition of virus replication. PKR can be activated by binding to dsRNA or cellular proteins such as PACT/RAX, or by its conjugation to ISG15 or SUMO. Here, we demonstrate that PKR also interacts with SUMO in a non-covalent manner. We identify the phosphorylable tyrosine residue 162 in PKR (Y162) as a modulator of the PKR-SUMO non-covalent interaction as well as of the PKR SUMOylation...
October 25, 2017: Scientific Reports
Fei Yu, Longlong Wang, Hao Wang, Jialu Sheng, Liqun Lu
SUMOylation, a post-translational modification, is involved in interaction between hosts and viruses, and participates in diverse cellular processes including inflammatory responses and innate immunity. Here, we investigated the interaction between reovirus infection and the cellular SUMOylation machinery using grass carp reovirus (GCRV) as a model. Full-length cDNAs of grass carp SUMO-1 and SUMO-2 were obtained and phylogenetic analysis indicated that they shared high homology with those of higher vertebrates...
September 22, 2017: Oncotarget
Jing Wang, Rong Deng, Nan Cui, Hailong Zhang, Tianqi Liu, Jinzhuo Dou, Xian Zhao, Ran Chen, Yanli Wang, Jianxiu Yu, Jian Huang
Src, a non-receptor tyrosine kinase protein, plays a critical role in cell proliferation and tumorigenesis. SUMOylation, a reversible ubiquitination-like post-translational modification, is vital for tumor progression. Here, we report that the Src protein can be SUMOylated at lysine 318 both in vitro and in vivo. Hypoxia can induce a decrease of Src SUMOylation along with an increase of Y419 phosphorylation, a phosphorylation event required for Src activation. On the other hand, treatment with hydrogen peroxide can enhance Src SUMOylation...
October 22, 2017: Neoplasia: An International Journal for Oncology Research
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