Journal articles: 'Sumoylome'

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Colignon, Bertrand, Edouard Delaive, Marc Dieu, Catherine Demazy, Yordan Muhovski, Cindy Wallon, Martine Raes, and Sergio Mauro. "Proteomics analysis of the endogenous, constitutive, leaf SUMOylome." Journal of Proteomics 150 (January 2017): 268–80. http://dx.doi.org/10.1016/j.jprot.2016.09.012.

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Horio, Tetsuya, Edyta Szewczyk, C. Elizabeth Oakley, Aysha H. Osmani, Stephen A. Osmani, and Berl R. Oakley. "SUMOlock reveals a more complete Aspergillus nidulans SUMOylome." Fungal Genetics and Biology 127 (June 2019): 50–59. http://dx.doi.org/10.1016/j.fgb.2019.03.002.

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Ingole, Kishor D., Shraddha K. Dahale, and Saikat Bhattacharjee. "Proteomic analysis of SUMO1-SUMOylome changes during defense elicitation in Arabidopsis." Journal of Proteomics 232 (February 2021): 104054. http://dx.doi.org/10.1016/j.jprot.2020.104054.

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Rytz, Thérèse C., Marcus J. Miller, Fionn McLoughlin, Robert C. Augustine, Richard S. Marshall, Yu-ting Juan, Yee-yung Charng, Mark Scalf, Lloyd M. Smith, and Richard D. Vierstra. "SUMOylome Profiling Reveals a Diverse Array of Nuclear Targets Modified by the SUMO Ligase SIZ1 during Heat Stress." Plant Cell 30, no. 5 (March 27, 2018): 1077–99. http://dx.doi.org/10.1105/tpc.17.00993.

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Zhao, Xu, Ivo A. Hendriks, Stéphanie Le Gras, Tao Ye, Lucía Ramos-Alonso, Aurélie Nguéa P, Guro Flor Lien, et al. "Waves of sumoylation support transcription dynamics during adipocyte differentiation." Nucleic Acids Research 50, no. 3 (January 31, 2022): 1351–69. http://dx.doi.org/10.1093/nar/gkac027.

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Abstract Tight control of gene expression networks required for adipose tissue formation and plasticity is essential for adaptation to energy needs and environmental cues. However, the mechanisms that orchestrate the global and dramatic transcriptional changes leading to adipocyte differentiation remain to be fully unraveled. We investigated the regulation of nascent transcription by the sumoylation pathway during adipocyte differentiation using SLAMseq and ChIPseq. We discovered that the sumoylation pathway has a dual function in differentiation; it supports the initial downregulation of pre-adipocyte-specific genes, while it promotes the establishment of the mature adipocyte transcriptional program. By characterizing endogenous sumoylome dynamics in differentiating adipocytes by mass spectrometry, we found that sumoylation of specific transcription factors like PPARγ/RXR and their co-factors are associated with the transcription of adipogenic genes. Finally, using RXR as a model, we found that sumoylation may regulate adipogenic transcription by supporting the chromatin occurrence of transcription factors. Our data demonstrate that the sumoylation pathway supports the rewiring of transcriptional networks required for formation of functional adipocytes. This study also provides the scientists in the field of cellular differentiation and development with an in-depth resource of the dynamics of the SUMO-chromatin landscape, SUMO-regulated transcription and endogenous sumoylation sites during adipocyte differentiation.

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Mustfa, Salman Ahmad, Mukesh Singh, Aamir Suhail, Gayatree Mohapatra, Smriti Verma, Debangana Chakravorty, Sarika Rana, et al. "SUMOylation pathway alteration coupled with downregulation of SUMO E2 enzyme at mucosal epithelium modulates inflammation in inflammatory bowel disease." Open Biology 7, no. 6 (June 2017): 170024. http://dx.doi.org/10.1098/rsob.170024.

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Post-translational modification pathways such as SUMOylation are integral to all cellular processes and tissue homeostasis. We investigated the possible involvement of SUMOylation in the epithelial signalling in Crohn's disease (CD) and ulcerative colitis (UC), the two major forms of inflammatory bowel disease (IBD). Initially in a murine model of IBD, induced by dextran–sulfate–sodium (DSS mice), we observed inflammation accompanied by a lowering of global SUMOylation of colonic epithelium. The observed SUMOylation alteration was due to a decrease in the sole SUMO E2 enzyme (Ubc9). Mass-spectrometric analysis revealed the existence of a distinct SUMOylome (SUMO-conjugated proteome) in DSS mice with alteration of key cellular regulators, including master kinase Akt1. Knocking-down of Ubc9 in epithelial cells resulted in dramatic activation of inflammatory gene expression, a phenomenon that acted via reduction in Akt1 and its SUMOylated form. Importantly, a strong decrease in Ubc9 and Akt1 was also seen in endoscopic biopsy samples ( N = 66) of human CD and UC patients. Furthermore, patients with maximum disease indices were always accompanied by severely lowered Ubc9 or SUMOylated-Akt1. Mucosal tissues with severely compromised Ubc9 function displayed higher levels of pro-inflammatory cytokines and compromised wound-healing markers. Thus, our results reveal an important and previously undescribed role for the SUMOylation pathway involving Ubc9 and Akt1 in modulation of epithelial inflammatory signalling in IBD.

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Niu, Qun, Wanxin Hou, Yinjie Yan, Shuzhang Sun, Yanyan Lin, Houshun Fang, Chunshuang Ma, et al. "Antileukemic effects of topoisomerase I inhibitors mediated by de-SUMOylase SENP1." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1868, no. 12 (December 2022): 166492. http://dx.doi.org/10.1016/j.bbadis.2022.166492.

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Cuijpers, Sabine A. G., Edwin Willemstein, Jan G. Ruppert, Daphne M. van Elsland, William C. Earnshaw, and Alfred C. O. Vertegaal. "Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner." Journal of Cell Science 133, no. 14 (June 26, 2020): jcs248591. http://dx.doi.org/10.1242/jcs.248591.

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ABSTRACTCell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is not clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we present a novel abscission mechanism. We identified chromokinesin KIF4A, which is adjacent to the midbody during cytokinesis, as being required for efficient abscission. KIF4A is regulated by post-translational modifications. We evaluated modification of KIF4A by the ubiquitin-like protein SUMO. We mapped lysine 460 in KIF4A as the SUMO acceptor site and employed CRISPR-Cas9-mediated genome editing to block SUMO conjugation of endogenous KIF4A. Failure to SUMOylate this site in KIF4A delayed cytokinesis. SUMOylation of KIF4A enhanced the affinity for the microtubule destabilizer stathmin 1 (STMN1). We here present a new level of abscission regulation through the dynamic interactions between KIF4A and STMN1 as controlled by SUMO modification of KIF4A.

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Neo, Shu Hui, Yoko Itahana, Jennifer Alagu, Mayumi Kitagawa, Alvin Kunyao Guo, Sang Hyun Lee, Kai Tang, and Koji Itahana. "TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification." Molecular and Cellular Biology 35, no. 16 (June 8, 2015): 2851–63. http://dx.doi.org/10.1128/mcb.01064-14.

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The tumor suppressor ARF enhances the SUMOylation of target proteins; however, the physiological function of ARF-mediated SUMOylation has been unclear due to the lack of a known, associated E3 SUMO ligase. Here we uncover TRIM28/KAP1 as a novel ARF-binding protein and SUMO E3 ligase for NPM1/B23. ARF and TRIM28 cooperate to SUMOylate NPM1, a nucleolar protein that regulates centrosome duplication and genomic stability. ARF-mediated SUMOylation of NPM1 was attenuated by TRIM28 depletion and enhanced by TRIM28 overexpression. Coexpression of ARF and TRIM28 promoted NPM1 centrosomal localization by enhancing its SUMOylation and suppressed centrosome amplification; these functions required the E3 ligase activity of TRIM28. Conversely, depletion of ARF or TRIM28 increased centrosome amplification. ARF also counteracted oncogenic Ras-induced centrosome amplification. Centrosome amplification is often induced by oncogenic insults, leading to genomic instability. However, the mechanisms employed by tumor suppressors to protect the genome are poorly understood. Our findings suggest a novel role for ARF in maintaining genome integrity by facilitating TRIM28-mediated SUMOylation of NPM1, thus preventing centrosome amplification.

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Sharma, Manish, and Srinivasa Subramaniam. "Rhes travels from cell to cell and transports Huntington disease protein via TNT-like protrusion." Journal of Cell Biology 218, no. 6 (May 10, 2019): 1972–93. http://dx.doi.org/10.1083/jcb.201807068.

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Tunneling nanotubes (TNT) are thin, membranous, tunnel-like cell-to-cell connections, but the mechanisms underlying their biogenesis or functional role remains obscure. Here, we report, Rhes, a brain-enriched GTPase/SUMO E3-like protein, induces the biogenesis of TNT-like cellular protrusions, “Rhes tunnels,” through which Rhes moves from cell to cell and transports Huntington disease (HD) protein, the poly-Q expanded mutant Huntingtin (mHTT). The formation of TNT-like Rhes tunnels requires the Rhes’s serine 33, C-terminal CAAX, and a SUMO E3-like domain. Electron microscopy analysis revealed that TNT-like Rhes tunnels appear continuous, cell–cell connections, and <200 nm in diameter. Live-cell imaging shows that Rhes tunnels establish contact with the neighboring cell and deliver Rhes-positive cargoes, which travel across the plasma membrane of the neighboring cell before entering it. The Rhes tunnels carry Rab5a/Lyso 20-positive vesicles and transport mHTT, but not normal HTT, mTOR, or wtTau proteins. SUMOylation-defective mHTT, Rhes C263S (cannot SUMOylate mHTT), or CRISPR/Cas9-mediated depletion of three isoforms of SUMO diminishes Rhes-mediated mHTT transport. Thus, Rhes promotes the biogenesis of TNT-like cellular protrusions and facilitates the cell–cell transport of mHTT involving SUMO-mediated mechanisms.

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Zhang, Junya, Robert C. Augustine, Masaharu Suzuki, Juanjuan Feng, Si Nian Char, Bing Yang, Donald R. McCarty, and Richard D. Vierstra. "The SUMO ligase MMS21 profoundly influences maize development through its impact on genome activity and stability." PLOS Genetics 17, no. 10 (October 25, 2021): e1009830. http://dx.doi.org/10.1371/journal.pgen.1009830.

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The post-translational addition of SUMO plays essential roles in numerous eukaryotic processes including cell division, transcription, chromatin organization, DNA repair, and stress defense through its selective conjugation to numerous targets. One prominent plant SUMO ligase is METHYL METHANESULFONATE-SENSITIVE (MMS)-21/HIGH-PLOIDY (HPY)-2/NON-SMC-ELEMENT (NSE)-2, which has been connected genetically to development and endoreduplication. Here, we describe the potential functions of MMS21 through a collection of UniformMu and CRISPR/Cas9 mutants in maize (Zea mays) that display either seed lethality or substantially compromised pollen germination and seed/vegetative development. RNA-seq analyses of leaves, embryos, and endosperm from mms21 plants revealed a substantial dysregulation of the maize transcriptome, including the ectopic expression of seed storage protein mRNAs in leaves and altered accumulation of mRNAs associated with DNA repair and chromatin dynamics. Interaction studies demonstrated that MMS21 associates in the nucleus with the NSE4 and STRUCTURAL MAINTENANCE OF CHROMOSOMES (SMC)-5 components of the chromatin organizer SMC5/6 complex, with in vitro assays confirming that MMS21 will SUMOylate SMC5. Comet assays measuring genome integrity, sensitivity to DNA-damaging agents, and protein versus mRNA abundance comparisons implicated MMS21 in chromatin stability and transcriptional controls on proteome balance. Taken together, we propose that MMS21-directed SUMOylation of the SMC5/6 complex and other targets enables proper gene expression by influencing chromatin structure.

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Liu, Yang, Ya-Dong Zhang, Liang Guo, Hai-Yan Huang, Hao Zhu, Jia-Xin Huang, Yuan Liu, et al. "Protein Inhibitor of Activated STAT 1 (PIAS1) Is Identified as the SUMO E3 Ligase of CCAAT/Enhancer-Binding Protein β (C/EBPβ) during Adipogenesis." Molecular and Cellular Biology 33, no. 22 (September 23, 2013): 4606–17. http://dx.doi.org/10.1128/mcb.00723-13.

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It is well recognized that PIAS1, a SUMO (small ubiquitin-like modifier) E3 ligase, modulates such cellular processes as cell proliferation, DNA damage responses, and inflammation responses. Recent studies have shown that PIAS1 also plays a part in cell differentiation. However, the role of PIAS1 in adipocyte differentiation remains unknown. CCAAT/enhancer-binding protein β (C/EBPβ), a major regulator of adipogenesis, is a target of SUMOylation, but the E3 ligase responsible for the SUMOylation of C/EBPβ has not been identified. The present study showed that PIAS1 functions as a SUMO E3 ligase of C/EBPβ to regulate adipogenesis. PIAS1 expression was significantly and transiently induced on day 4 of 3T3-L1 adipocyte differentiation, when C/EBPβ began to decline. PIAS1 was found to interact with C/EBPβ through the SAP (scaffold attachment factor A/B/acinus/PIAS) domain and SUMOylate it, leading to increased ubiquitination and degradation of C/EBPβ. C/EBPβ became more stable when PIAS1 was silenced by RNA interference (RNAi). Moreover, adipogenesis was inhibited by overexpression of wild-type PIAS1 and promoted by knockdown of PIAS1. The mutational study indicated that the catalytic activity of SUMO E3 ligase was required for PIAS1 to restrain adipogenesis. Importantly, the inhibitory effect of PIAS1 overexpression on adipogenesis was rescued by overexpressed C/EBPβ. Thus, PIAS1 could play a dynamic role in adipogenesis by promoting the SUMOylation of C/EBPβ.

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Srivastav, Ratnesh K., Susan Schwede, Malte Klaus, Jessica Schwermann, Matthias Gaestel, and Rainer Niedenthal. "Monitoring protein–protein interactions in mammalian cells by trans-SUMOylation." Biochemical Journal 438, no. 3 (August 26, 2011): 495–503. http://dx.doi.org/10.1042/bj20110035.

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Protein–protein interactions are essential for almost all cellular processes, hence understanding these processes mainly depends on the identification and characterization of the relevant protein–protein interactions. In the present paper, we introduce the concept of TRS (trans-SUMOylation), a new method developed to identify and verify protein–protein interactions in mammalian cells in vivo. TRS utilizes Ubc9-fusion proteins that trans-SUMOylate co-expressed interacting proteins. Using TRS, we analysed interactions of 65 protein pairs co-expressed in HEK (human embryonic kidney)-293 cells. We identified seven new and confirmed 16 known protein interactions, which were determined via endogenous SUMOylation sites of the binding partners or by using SUMOylation-site tags respectively. Four of the new protein interactions were confirmed by GST (glutathione transferase) pull-down and the p38α–Edr2 interaction was verified by co-localization analysis. Functionally, this p38α–Edr2 interaction could possibly be involved in the recruitment of p38α to the polycomb chromatin-remodelling complex to phosphorylate Bmi1. We also used TRS to characterize protein-interaction domains of the protein kinase pairs p38α–MK2 [MK is MAPK (mitogen-activated protein kinase)-activated protein kinase] and ERK3 (extracellular-signal-regulated kinase 3)–MK5 and of the p38α–p53 complex. The ability of TRS to monitor protein interactions in mammalian cells in vivo at levels similar to endogenous expression makes it an excellent new tool that can help in defining the protein interactome of mammalian cells.

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Du, Qian, Lei Zhu, Jianhui Zhong, Xueqi Wei, Qi Zhang, Tengfei Shi, Cong Han, et al. "Porcine circovirus type 2 infection promotes the SUMOylation of nucleophosmin-1 to facilitate the viral circular single-stranded DNA replication." PLOS Pathogens 20, no. 2 (February 23, 2024): e1012014. http://dx.doi.org/10.1371/journal.ppat.1012014.

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The mechanism of genome DNA replication in circular single-stranded DNA viruses is currently a mystery, except for the fact that it undergoes rolling-circle replication. Herein, we identified SUMOylated porcine nucleophosmin-1 (pNPM1), which is previously reported to be an interacting protein of the viral capsid protein, as a key regulator that promotes the genome DNA replication of porcine single-stranded DNA circovirus. Upon porcine circovirus type 2 (PCV2) infection, SUMO2/3 were recruited and conjugated with the K263 site of pNPM1’s C-terminal domain to SUMOylate pNPM1, subsequently, the SUMOylated pNPM1 were translocated in nucleoli to promote the replication of PCV2 genome DNA. The mutation of the K263 site reduced the SUMOylation levels of pNPM1 and the nucleolar localization of pNPM1, resulting in a decrease in the level of PCV2 DNA replication. Meanwhile, the mutation of the K263 site prevented the interaction of pNPM1 with PCV2 DNA, but not the interaction of pNPM1 with PCV2 Cap. Mechanistically, PCV2 infection increased the expression levels of Ubc9, the only E2 enzyme involved in SUMOylation, through the Cap-mediated activation of ERK signaling. The upregulation of Ubc9 promoted the interaction between pNPM1 and TRIM24, a potential E3 ligase for SUMOylation, thereby facilitating the SUMOylation of pNPM1. The inhibition of ERK activation could significantly reduce the SUMOylation levels and the nucleolar localization of pNPM1, as well as the PCV2 DNA replication levels. These results provide new insights into the mechanism of circular single-stranded DNA virus replication and highlight NPM1 as a potential target for inhibiting PCV2 replication.

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MA, Jiao, Bin Liu, Dan Yu, Wayne Tam, Jianmin Yang, and Jinke Cheng. "SIRT3 Sumoylation Contributes to Chemoresistance in AML." Blood 132, Supplement 1 (November 29, 2018): 3929. http://dx.doi.org/10.1182/blood-2018-99-110898.

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Abstract Acute myeloid leukemia (AML) is a clonal disease originated from a rare population of malignant hematopoietic cells, called leukemic stem cells (LSCs), which is not only often resistant to standard chemotherapies, but also the major cause of relapse and eventual death of AML patients. The five-year survival of AML keeps as low as 27% for the last few decades. LSCs possess unique metabolism profiles such as higher rates of oxidative phosphorylation, and dependence on fatty acid oxidation for survival, which is distinct from normal hematopoietic cells, and, as a consequence, relatively low level of reactive oxygen species (ROS), a critical regulator for stemness maintenance. Therefore, targeting mitochondrial metabolism, especially ROS, may be a promising strategy to improve chemotherapy outcome for AML. We have previously found in hepatocarcinoma cells that SUMOylation is one of the important post-translational modifications for a variety of cellular proteins, and is capable of regulating the enzymatic activity of some key mitochondrial enzymes involved in the metabolic control, one example of which is SIRT3, a NAD+-dependent protein deacetylase. SIRT3 is reported to influence cellular metabolism and downregulate ROS generation by deacetylating mitochondrial anti-oxidant enzymes. The targets of SIRT3 include superoxide dismutase 2 (SOD2), manganese superoxide dismutase (MnSOD) and isocitrate dehydrogenase 2 (IDH2), which have been shown closely related to leukemogenesis. Since sophisticated regulation of ROS production is required for the maintenance of LSCs, we reproduced SUMOylation of SIRT3, and investigated its role in the mitochondrial metabolism in AML. In fact, SIRT3 SUMOylation at lysine 288 was also found in AML cells. To reveal the consequences of SIRT3 SUMOylation in AML, we constructed a plasmid expressing SIRT3-K288R that fails to be SUMOylated in AML cells. As a result, AML cells expressing SIRT3-K288R protected AML cells from as shown by apoptotic assays and quantitation of activated caspase 3 via reduction of not only total but also mitochondrial ROS production under chemotherapeutic agent-induced cell death comparing to those transfected with vector or overexpressing wild type SIRT3. To further investigate the role of SIRT3 de-SUMOylation in AML, we examined the influence of mitochondrial metabolism and anti-oxidant enzymes by SIRT3-K288R. SIRT3-K288R significantly downregulated the acetylation of mitochondrial anti-oxidant enzymes, such as SOD2, leading to decreased NADP/NADPH ratio and increased GSH/GSSG ratio. SIRT3 de-SUMOylation enhanced OCR but impaired ECAR under both basic and cytarabine treated conditions. We analyzed 18 primary AML samples to evaluate the correlation among SIRT3 SUMOylation, ROS level and chemoresistance. As we expected, low level of SIRT3 SUMOylation correlates with low cellular ROS level in both bulk AML and CD34+CD38- AML stem cells, and less sensitivity to cytarabine. Furthermore, MV4-11 cells bearing control vector, wild type SIRT3 or SIRT3-K288R were engrafted in NSG mice. Cytarabine was administered to the xenografts to evaluate the chemoresistance in these cell line-derived xenograft (CDX) mouse models. Consistent to the in vitro data, SIRT3-K288R reduced total and mitochondrial ROS in vivo, resulted in enhanced leukemogenesis and impaired survival. Taken together, our study showed that SIRT3 can be SUMOylated in AML. De-SUMOylation enhances SIRT3 deacetylase activity, and contribute to the chemoresistance of AML cells via altered mitochondrial metabolism and reduced ROS generation. Thus, SIRT3 and its de-SUMOylase can be utilized as potential therapeutic targets to improve AML chemotherapy. Disclosures No relevant conflicts of interest to declare.

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Kasera, Mritunjay, Kishor D. Ingole, Sakshi Rampuria, Yashika Walia, Walter Gassmann, and Saikat Bhattacharjee. "Global SUMOylome Adjustments in Basal Defenses of Arabidopsis thaliana Involve Complex Interplay Between SMALL-UBIQUITIN LIKE MODIFIERs and the Negative Immune Regulator SUPPRESSOR OF rps4-RLD1." Frontiers in Cell and Developmental Biology 9 (September 30, 2021). http://dx.doi.org/10.3389/fcell.2021.680760.

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Steady-state SUMOylome of a plant is adjusted locally during developmental transitions and more globally during stress exposures. We recently reported that basal immunity in Arabidopsis thaliana against Pseudomonas syringae pv tomato strain DC3000 (PstDC3000) is associated with strong enhancements in the net SUMOylome. Transcriptional upregulations of SUMO conjugases, suppression of protease, and increased SUMO translations accounted for this enhanced SUMOylation. Antagonistic roles of SUMO1/2 and SUMO3 isoforms further fine-tuned the SUMOylome adjustments, thus impacting defense amplitudes and immune outcomes. Loss of function of SUPPRESSOR OF rps4-RLD1 (SRFR1), a previously reported negative regulator of basal defenses, also caused constitutive increments in global SUMO-conjugates through similar modes. These suggest that SRFR1 plays a pivotal role in maintenance of SUMOylation homeostasis and its dynamic changes during immune elicitations. Here, we demonstrate that SRFR1 degradation kinetically precedes and likely provides the salicylic acid (SA) elevations necessary for the SUMOylome increments in basal defenses. We show that SRFR1 not only is a SUMOylation substrate but also interacts in planta with both SUMO1 and SUMO3. In sum1 or sum3 mutants, SRFR1 stabilities are reduced albeit by different modes. Whereas a srfr1 sum1 combination is lethal, the srfr1 sum3 plants retain developmental defects and enhanced immunity of the srfr1 parent. Together with increasing evidence of SUMOs self-regulating biochemical efficiencies of SUMOylation-machinery, we present their impositions on SRFR1 expression that in turn counter-modulates the SUMOylome. Overall, our investigations reveal multifaceted dynamics of regulated SUMOylome changes via SRFR1 in defense-developmental balance.

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Pronot, Marie, Félicie Kieffer, Anne-Sophie Gay, Delphine Debayle, Raphaël Forquet, Gwénola Poupon, Lenka Schorova, Stéphane Martin, and Carole Gwizdek. "Proteomic Identification of an Endogenous Synaptic SUMOylome in the Developing Rat Brain." Frontiers in Molecular Neuroscience 14 (November 23, 2021). http://dx.doi.org/10.3389/fnmol.2021.780535.

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Synapses are highly specialized structures that interconnect neurons to form functional networks dedicated to neuronal communication. During brain development, synapses undergo activity-dependent rearrangements leading to both structural and functional changes. Many molecular processes are involved in this regulation, including post-translational modifications by the Small Ubiquitin-like MOdifier SUMO. To get a wider view of the panel of endogenous synaptic SUMO-modified proteins in the mammalian brain, we combined subcellular fractionation of rat brains at the post-natal day 14 with denaturing immunoprecipitation using SUMO2/3 antibodies and tandem mass spectrometry analysis. Our screening identified 803 candidate SUMO2/3 targets, which represents about 18% of the synaptic proteome. Our dataset includes neurotransmitter receptors, transporters, adhesion molecules, scaffolding proteins as well as vesicular trafficking and cytoskeleton-associated proteins, defining SUMO2/3 as a central regulator of the synaptic organization and function.

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Sharma, Komal, Irina Sizova, Sibaji K. Sanyal, Girdhar K. Pandey, Peter Hegemann, and Suneel Kateriya. "Deciphering the role of cytoplasmic domain of Channelrhodopsin in modulating the interactome and SUMOylome of Chlamydomonas reinhardtii." International Journal of Biological Macromolecules, May 2023, 125135. http://dx.doi.org/10.1016/j.ijbiomac.2023.125135.

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Condezo, Yazmine B., Raquel Sainz-Urruela, Laura Gomez-H, Daniel Salas-Lloret, Natalia Felipe-Medina, Rachel Bradley, Ian D. Wolff, et al. "RNF212B E3 ligase is essential for crossover designation and maturation during male and female meiosis in the mouse." Proceedings of the National Academy of Sciences 121, no. 25 (June 12, 2024). http://dx.doi.org/10.1073/pnas.2320995121.

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Meiosis, a reductional cell division, relies on precise initiation, maturation, and resolution of crossovers (COs) during prophase I to ensure the accurate segregation of homologous chromosomes during metaphase I. This process is regulated by the interplay of RING-E3 ligases such as RNF212 and HEI10 in mammals. In this study, we functionally characterized a recently identified RING-E3 ligase, RNF212B. RNF212B colocalizes and interacts with RNF212, forming foci along chromosomes from zygonema onward in a synapsis-dependent and DSB-independent manner. These consolidate into larger foci at maturing COs, colocalizing with HEI10, CNTD1, and MLH1 by late pachynema. Genetically, RNF212B foci formation depends on Rnf212 but not on Msh4 , Hei10, and Cntd1 , while the unloading of RNF212B at the end of pachynema is dependent on Hei10 and Cntd1 . Mice lacking RNF212B, or expressing an inactive RNF212B protein, exhibit modest synapsis defects, a reduction in the localization of pro-CO factors (MSH4, TEX11, RPA, MZIP2) and absence of late CO-intermediates (MLH1). This loss of most COs by diakinesis results in mostly univalent chromosomes. Double mutants for Rnf212b and Rnf212 exhibit an identical phenotype to that of Rnf212b single mutants, while double heterozygous demonstrate a dosage-dependent reduction in CO number, indicating a functional interplay between paralogs. SUMOylome analysis of testes from Rnf212b mutants and pull-down analysis of Sumo- and Ubiquitin-tagged HeLa cells, suggest that RNF212B is an E3-ligase with Ubiquitin activity, serving as a crucial factor for CO maturation. Thus, RNF212 and RNF212B play vital, yet overlapping roles, in ensuring CO homeostasis through their distinct E3 ligase activities.

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Yang, Qi, Jielin Tang, Chonghui Xu, He Zhao, Yuan Zhou, Yanyi Wang, Min Yang, Xinwen Chen, and Jizheng Chen. "Histone deacetylase 4 inhibits NF-κB activation by facilitating IκBα sumoylation." Journal of Molecular Cell Biology, August 8, 2020. http://dx.doi.org/10.1093/jmcb/mjaa043.

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Abstract Protein modification by SUMO (small ubiquitin-like modifier) is an important regulatory mechanism for multiple cellular processes. While the canonical pathway involving the ubiquitylation or phosphorylation of IκBα has been well characterized, little is known about the sumoylation of IκBα in the control of NF-κB activity. Here we find that HDAC4 negatively regulates TNFα or LPS triggered NF-κB activation. HDAC4 belongs to the SUMO E3 ligase family and can directly sumoylate IκBα. The cytoplasm location of HDAC4 is essential for IκBα sumoylation. The cysteine 292 of HDAC4 is a key site for its sumo E3 ligase activity. The sumoylation of IκBα prevents its poly-ubiquitination and degradation because these two modifications occur both at the Lys21. Our findings reveal a previously undiscovered role for HDAC4 in the inflammatory response as a sumo E3 ligase for IκBα sumoylation. Our work provides insight into mechanisms ensuring optimal mediation of the NF-κB pathway.

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Ma, Xiaoyu, Yingyi Zhang, Yuanyuan Zhang, Xu Zhang, Yan Huang, Kai He, Chuan Chen, et al. "A stress-induced cilium-to-PML-NB route drives senescence initiation." Nature Communications 14, no. 1 (April 3, 2023). http://dx.doi.org/10.1038/s41467-023-37362-7.

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AbstractCellular senescence contributes to tissue homeostasis and age-related pathologies. However, how senescence is initiated in stressed cells remains vague. Here, we discover that exposure to irradiation, oxidative or inflammatory stressors induces transient biogenesis of primary cilia, which are then used by stressed cells to communicate with the promyelocytic leukemia nuclear bodies (PML-NBs) to initiate senescence responses in human cells. Mechanistically, a ciliary ARL13B-ARL3 GTPase cascade negatively regulates the association of transition fiber protein FBF1 and SUMO-conjugating enzyme UBC9. Irreparable stresses downregulate the ciliary ARLs and release UBC9 to SUMOylate FBF1 at the ciliary base. SUMOylated FBF1 then translocates to PML-NBs to promote PML-NB biogenesis and PML-NB-dependent senescence initiation. Remarkably, Fbf1 ablation effectively subdues global senescence burden and prevents associated health decline in irradiation-treated mice. Collectively, our findings assign the primary cilium a key role in senescence induction in mammalian cells and, also, a promising target in future senotherapy strategies.

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Wang, Li, Wenjing Zeng, Chaowen Wang, Yanli Lu, Xiaowei Xiong, Sheng Chen, Qianqian Huang, Feixing Yan, and Qiren Huang. "SUMOylation and coupling of eNOS mediated by PIAS1 contribute to maintenance of vascular homeostasis." FASEB Journal 38, no. 1 (December 16, 2023). http://dx.doi.org/10.1096/fj.202301963r.

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AbstractEndothelial dysfunction (ED) is commonly considered a crucial initiating step in the pathogenesis of numerous cardiovascular diseases. The coupling of endothelial nitric oxide synthase (eNOS) is important in maintaining normal endothelial functions. However, it still remains elusive whether and how eNOS SUMOylation affects the eNOS coupling. In the study, we investigate the roles and possible action mechanisms of protein inhibitor of activated STAT 1 (PIAS1) in ED. Human umbilical vein endothelial cells (HUVECs) treated with palmitate acid (PA) in vitro and ApoE−/− mice fed with high‐fat diet (HFD) in vivo were constructed as the ED models. Our in vivo data show that PIAS1 alleviates the dysfunction of vascular endothelium by increasing nitric oxide (NO) level, reducing malondialdehyde (MDA) level, and activating the phosphatidylinositol 3‐kinase‐protein kinase B‐endothelial nitric oxide synthase (PI3K‐AKT‐eNOS) signaling in ApoE−/− mice. Our in vitro data also show that PIAS1 can SUMOylate eNOS under endogenous conditions; moreover, it antagonizes the eNOS uncoupling induced by PA. The findings demonstrate that PIAS1 alleviates the dysfunction of vascular endothelium by promoting the SUMOylation and inhibiting the uncoupling of eNOS, suggesting that PIAS1 would become an early predictor of atherosclerosis and a new potential target of the hyperlipidemia‐related cardiovascular diseases.

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Journal articles on the topic 'Sumoylome'

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