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Artykuły w czasopismach na temat „SUMO Protease”

Autor: Grafiati

Data publikacji: 6 września 2023

Data aktualizacji: 19 lipca 2025

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1

Yang, Wei, Liangli Wang, and Wulf Paschen. "Development of a High-Throughput Screening Assay for Inhibitors of Small Ubiquitin-Like Modifier Proteases." Journal of Biomolecular Screening 18, no. 5 (2013): 621–28. http://dx.doi.org/10.1177/1087057113479971.

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Small ubiquitin-like modifier (SUMO1–3) is a small group of proteins that are ligated to lysine residues in target proteins. SUMO conjugation is a highly dynamic process, as SUMOylated proteins are rapidly deconjugated by SUMO proteases. SUMO conjugation/deconjugation plays pivotal roles in major cellular pathways and is associated with a number of pathological conditions. It is therefore of significant clinical interest to develop new strategies to screen for compounds to specifically interfere with SUMO conjugation/deconjugation. Here, we describe a novel high-throughput screening (HTS)–comp

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2

Mukhopadhyay, Debaditya, Ferhan Ayaydin, Nagamalleswari Kolli, et al. "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species." Journal of Cell Biology 174, no. 7 (2006): 939–49. http://dx.doi.org/10.1083/jcb.200510103.

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Small ubiquitin-related modifier (SUMO) processing and deconjugation are mediated by sentrin-specific proteases/ubiquitin-like proteases (SENP/Ulps). We show that SUMO-specific protease 1 (SUSP1), a mammalian SENP/Ulp, localizes within the nucleoplasm. SUSP1 depletion within cell lines expressing enhanced green fluorescent protein (EGFP) fusions to individual SUMO paralogues caused redistribution of EGFP-SUMO2 and -SUMO3, particularly into promyelocytic leukemia (PML) bodies. Further analysis suggested that this change resulted primarily from a deficit of SUMO2/3-deconjugation activity. Under

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3

Alegre, Kamela O., and David Reverter. "Swapping Small Ubiquitin-like Modifier (SUMO) Isoform Specificity of SUMO Proteases SENP6 and SENP7." Journal of Biological Chemistry 286, no. 41 (2011): 36142–51. http://dx.doi.org/10.1074/jbc.m111.268847.

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SUMO proteases can regulate the amounts of SUMO-conjugated proteins in the cell by cleaving off the isopeptidic bond between SUMO and the target protein. Of the six members that constitute the human SENP/ULP protease family, SENP6 and SENP7 are the most divergent members in their conserved catalytic domain. The SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/3 isoforms. To investigate the structural determinants for such isoform specificity, we have identified a unique sequence insertion in the SENP6 and SENP7 subclass that is essential for their proteolytic

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4

Liu, Yan, Yali Shen, Yang Song, Lei Xu, J. Jefferson P. P. Perry, and Jiayu Liao. "Isopeptidase Kinetics Determination by a Real Time and Sensitive qFRET Approach." Biomolecules 11, no. 5 (2021): 673. http://dx.doi.org/10.3390/biom11050673.

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Isopeptidase activity of proteases plays critical roles in physiological and pathological processes in living organisms, such as protein stability in cancers and protein activity in infectious diseases. However, the kinetics of protease isopeptidase activity has not been explored before due to a lack of methodology. Here, we report the development of novel qFRET-based protease assay for characterizing the isopeptidase kinetics of SENP1. The reversible process of SUMOylation in vivo requires an enzymatic cascade that includes E1, E2, and E3 enzymes and Sentrin/SUMO-specific proteases (SENPs), w

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5

Shen, Lin Nan, Changjiang Dong, Huanting Liu, James H. Naismith, and Ronald T. Hay. "The structure of SENP1–SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing." Biochemical Journal 397, no. 2 (2006): 279–88. http://dx.doi.org/10.1042/bj20052030.

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The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between S

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6

Xu, Zheng, So Fun Chau, Kwok Ho Lam, Ho Yin Chan, Tzi Bun Ng, and Shannon W. N. Au. "Crystal structure of the SENP1 mutant C603S–SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease." Biochemical Journal 398, no. 3 (2006): 345–52. http://dx.doi.org/10.1042/bj20060526.

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SUMO (small ubiquitin-related modifier)-specific proteases catalyse the maturation and de-conjugation processes of the sumoylation pathway and modulate various cellular responses including nuclear metabolism and cell cycle progression. The active-site cysteine residue is conserved among all known SUMO-specific proteases and is not substitutable by serine in the hydrolysis reactions demonstrated previously in yeast. We report here that the catalytic domain of human protease SENP1 (SUMO-specific protease 1) mutant SENP1CC603S carrying a mutation of cysteine to serine at the active site is inacti

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7

Di Bacco, Alessandra, Jian Ouyang, Hsiang-Ying Lee, Andre Catic, Hidde Ploegh, and Grace Gill. "The SUMO-Specific Protease SENP5 Is Required for Cell Division." Molecular and Cellular Biology 26, no. 12 (2006): 4489–98. http://dx.doi.org/10.1128/mcb.02301-05.

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ABSTRACT Posttranslational modification of substrates by the small ubiquitin-like modifier, SUMO, regulates diverse biological processes, including transcription, DNA repair, nucleocytoplasmic trafficking, and chromosome segregation. SUMOylation is reversible, and several mammalian homologs of the yeast SUMO-specific protease Ulp1, termed SENPs, have been identified. We demonstrate here that SENP5, a previously uncharacterized Ulp1 homolog, has SUMO C-terminal hydrolase and SUMO isopeptidase activities. In contrast to other SENPs, the C-terminal catalytic domain of SENP5 preferentially process

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8

Lee, Jiwon, Yool Lee, Min Joo Lee, et al. "Dual Modification of BMAL1 by SUMO2/3 and Ubiquitin Promotes Circadian Activation of the CLOCK/BMAL1 Complex." Molecular and Cellular Biology 28, no. 19 (2008): 6056–65. http://dx.doi.org/10.1128/mcb.00583-08.

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ABSTRACT Heterodimers of BMAL1 and CLOCK drive rhythmic expression of clock-controlled genes, thereby generating circadian physiology and behavior. Posttranslational modifications of BMAL1 play a key role in modulating the transcriptional activity of the CLOCK/BMAL1 complex during the circadian cycle. Recently, we demonstrated that circadian activation of the heterodimeric transcription factor is accompanied by ubiquitin-dependent proteolysis of BMAL1. Here we show that modification by SUMO localizes BMAL1 exclusively to the promyelocytic leukemia nuclear body (NB) and simultaneously promotes

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9

Dorval, Véronique, Matthew J. Mazzella, Paul M. Mathews, Ronald T. Hay та Paul E. Fraser. "Modulation of Aβ generation by small ubiquitin-like modifiers does not require conjugation to target proteins". Biochemical Journal 404, № 2 (2007): 309–16. http://dx.doi.org/10.1042/bj20061451.

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The sequential processing of the APP (amyloid precursor protein) by the β- and γ-secretase and generation of the Aβ (amyloid-β) peptide is a primary pathological factor in AD (Alzheimer's disease). Regulation of the processing or turnover of these proteins represents potential targets for the development of AD therapies. Sumoylation is a process by which SUMOs (small ubiquitin-like modifiers) are covalently conjugated to target proteins, resulting in a number of functional consequences. These include regulation of protein–protein interactions, intracellular trafficking and protein stability, w

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10

Roden, Julie, Leah Eardley, Andrew Hotson, Yajuan Cao, and Mary Beth Mudgett. "Characterization of the Xanthomonas AvrXv4 Effector, a SUMO Protease Translocated into Plant Cells." Molecular Plant-Microbe Interactions® 17, no. 6 (2004): 633–43. http://dx.doi.org/10.1094/mpmi.2004.17.6.633.

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Homologs of the Yersinia virulence factor YopJ are found in both animal and plant bacterial pathogens, as well as in plant symbionts. The conservation of this effector family indicates that several pathogens may use YopJ-like proteins to regulate bacteria-host interactions during infection. YopJ and YopJ-like proteins share structural homology with cysteine proteases and are hypothesized to functionally mimic small ubiquitin-like modifier (SUMO) proteases in eukaryotic cells. Strains of the phytopathogenic bacterium Xanthomonas campestris pv. vesicatoria are known to possess four YopJ-like pro

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11

XU, Zheng, and Shannon W. N. AU. "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1." Biochemical Journal 386, no. 2 (2005): 325–30. http://dx.doi.org/10.1042/bj20041210.

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SUMO (small ubiquitin-related modifier) is a member of the ubiquitin-like protein family that regulates cellular function of a variety of target proteins. SUMO proteins are expressed as their precursor forms. Cleavage of the residues after the ‘GG’ region of these precursors by SUMO-specific proteases in maturation is a prerequisite for subsequent sumoylation. To understand further this proteolytic processing, we expressed and purified SENP1 (sentrin-specific protease 1), one of the SUMO-specific proteases, using an Escherichia coli expression system. We show that SENP1 is capable of processin

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12

Kroetz, Mary B., Dan Su, and Mark Hochstrasser. "Essential Role of Nuclear Localization for Yeast Ulp2 SUMO Protease Function." Molecular Biology of the Cell 20, no. 8 (2009): 2196–206. http://dx.doi.org/10.1091/mbc.e08-10-1090.

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The SUMO protein is covalently attached to many different substrates throughout the cell. This modification is rapidly reversed by SUMO proteases. The Saccharomyces cerevisiae SUMO protease Ulp2 is a nuclear protein required for chromosome stability and cell cycle restart after checkpoint arrest. Ulp2 is related to the human SENP6 protease, also a nuclear protein. All members of the Ulp2/SENP6 family of SUMO proteases have large but poorly conserved N-terminal domains (NTDs) adjacent to the catalytic domain. Ulp2 also has a long C-terminal domain (CTD). We show that CTD deletion has modest eff

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13

Vertegaal, Alfred C. O. "SUMO chains: polymeric signals." Biochemical Society Transactions 38, no. 1 (2010): 46–49. http://dx.doi.org/10.1042/bst0380046.

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Ubiquitin and ubiquitin-like proteins are conjugated to a wide variety of target proteins that play roles in all biological processes. Target proteins are conjugated to ubiquitin monomers or to ubiquitin polymers that form via all seven internal lysine residues of ubiquitin. The fate of these target proteins is controlled in a chain architecture-dependent manner. SUMO (small ubiquitin-related modifier) shares the ability of ubiquitin to form chains via internal SUMOylation sites. Interestingly, a SUMO-binding site in Ubc9 is important for SUMO chain synthesis. Similar to ubiquitin–polymer clea

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14

Peek, Jennifer, Catherine Harvey, Dreux Gray, et al. "SUMO targeting of a stress-tolerant Ulp1 SUMO protease." PLOS ONE 13, no. 1 (2018): e0191391. http://dx.doi.org/10.1371/journal.pone.0191391.

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15

Elmore, Zachary C., Megan Donaher, Brooke C. Matson, Helen Murphy, Jason W. Westerbeck, and Oliver Kerscher. "Sumo-dependent substrate targeting of the SUMO protease Ulp1." BMC Biology 9, no. 1 (2011): 74. http://dx.doi.org/10.1186/1741-7007-9-74.

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Cheng, Jialin, Min Su, Yunfeng Jin, et al. "Upregulation of SENP3/SMT3IP1 promotes epithelial ovarian cancer progression and forecasts poor prognosis." Tumor Biology 39, no. 3 (2017): 101042831769454. http://dx.doi.org/10.1177/1010428317694543.

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As a crucial member of the small ubiquitin-like modifier system, SUMO-specific protease 3, was identified to be essential for cell proliferation and ribosomal RNA processing. Recent studies showed that SUMO-specific protease 3 was elevated in ovarian cancer compared to normal tissue samples. However, the connection between SUMO-specific protease 3-specific expression and clinicopathological parameters of epithelial ovarian cancer, as well as the physiologically potential role of SUMO-specific protease 3 in epithelial ovarian cancer remained unclear. In this study, an analysis of 124 paraffin-e

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17

Kang, Heejung, Eui Tae Kim, Hye-Ra Lee, et al. "Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein." Journal of General Virology 87, no. 8 (2006): 2181–90. http://dx.doi.org/10.1099/vir.0.81787-0.

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In human cytomegalovirus-infected cells, the immediate-early IE1 protein disrupts the subnuclear structures known as the PML oncogenic domains or PODs, via the induction of PML desumoylation. This activity correlates with the functions of IE1 in transcriptional regulation and in the stimulation of lytic infection. Here, the effects of IE1 in induction of desumoylation of PML were characterized. IE1 did not interfere with the formation of sumoylated forms of PML in vitro. In in vitro assays using the sumoylated proteins, a SUMO-specific protease SENP1 desumoylated both PML and IE1. However, the

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18

Klymkovych, I.-M. M. "USE OF SUMO-EXPRESSION SYSTEM AND SUMO-PROTEASE FOR PRODUCTION OF ACTIVE INTERFERON α-2b". Biotechnologia Acta 17, № 2 (2024): 54–55. http://dx.doi.org/10.15407/biotech17.02.054.

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Recombinant proteins production in prokaryotic expression systems is often complicated by need of native, N-terminal formylmethionine free molecule extraction, refolding, and processing. To facilitate these stages, alternative expression systems and fusion of target proteins are being used, in particular the SUMO system. Aim. This research aimed to verify a feasibility of SUMO-protease and SUMO-expression system using to produce active interferon α-2b. The goal was to increase both expression and total yield of the target protein and enhance its quality characteristics, particularly its purity

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19

Au, S. W., Z. Xu, K. H. Lam, and C. S. F. Chau. "Differential maturation of SUMO precursors by SUMO-specific protease, SENP1." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (2005): c208. http://dx.doi.org/10.1107/s0108767305091142.

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Liu, Linpo, Ying Jiang, Xiaomei Zhang, et al. "Two SUMO Proteases SUMO PROTEASE RELATED TO FERTILITY1 and 2 Are Required for Fertility in Arabidopsis." Plant Physiology 175, no. 4 (2017): 1703–19. http://dx.doi.org/10.1104/pp.17.00021.

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Schuldt, Alison. "A SUMO protease for stress protection." Nature Reviews Molecular Cell Biology 14, no. 5 (2013): 263. http://dx.doi.org/10.1038/nrm3569.

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Itahana, Yoko, Edward T. H. Yeh, and Yanping Zhang. "Nucleocytoplasmic Shuttling Modulates Activity and Ubiquitination-Dependent Turnover of SUMO-Specific Protease 2." Molecular and Cellular Biology 26, no. 12 (2006): 4675–89. http://dx.doi.org/10.1128/mcb.01830-05.

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ABSTRACT Small ubiquitin-related modifier (SUMO) proteins are conjugated to numerous polypeptides in cells, and attachment of SUMO plays important roles in regulating the activity, stability, and subcellular localization of modified proteins. SUMO modification of proteins is a dynamic and reversible process. A family of SUMO-specific proteases catalyzes the deconjugation of SUMO-modified proteins. Members of the Sentrin (also known as SUMO)-specific protease (SENP) family have been characterized with unique subcellular localizations. However, little is known about the functional significance o

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Nait Achour, Thiziri, Stéphanie Sentis, Catherine Teyssier та ін. "Transcriptional Repression of Estrogen Receptor α Signaling by SENP2 in Breast Cancer Cells". Molecular Endocrinology 28, № 2 (2014): 183–96. http://dx.doi.org/10.1210/me.2013-1376.

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Abstract Estrogen receptors (ERs) are ligand-activated transcription factors involved in many physiological and pathological processes, including breast cancer. Their activity is fine-tuned by posttranslational modifications, notably sumoylation. In the present study, we investigated the role of the small ubiquitin-related modifier (SUMO) protease, SUMO1/sentrin/suppressor of Mif 2-specific peptidase 2 (SENP2), in the regulation of ERα activity. We first found SENP2 to significantly repress estradiol-induced transcriptional activity in breast cancer cells (MCF7 and T47D). This effect was obser

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Liu, Yan, Yali Shen, Shasha Zheng, and Jiayu Liao. "A novel robust quantitative Förster resonance energy transfer assay for protease SENP2 kinetics determination against its all natural substrates." Molecular BioSystems 11, no. 12 (2015): 3407–14. http://dx.doi.org/10.1039/c5mb00568j.

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SUMOylation (the process of adding the SUMO [small ubiquitin-like modifier] to substrates) is an important post-translational modification of critical proteins in multiple processes. The kinetics parameters of pre-SUMO1-3 by its protease SENP2 is determined by a quantitative FRET assay in real time.

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Hattersley, Neil, Linnan Shen, Ellis G. Jaffray, and Ronald T. Hay. "The SUMO protease SENP6 is a direct regulator of PML nuclear bodies." Molecular Biology of the Cell 22, no. 1 (2011): 78–90. http://dx.doi.org/10.1091/mbc.e10-06-0504.

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Promyelocytic leukemia protein (PML) is the core component of PML-nuclear bodies (PML NBs). The small ubiquitin-like modifier (SUMO) system (and, in particular, SUMOylation of PML) is a critical component in the formation and regulation of PML NBs. SUMO protease SENP6 has been shown previously to be specific for SUMO-2/3–modified substrates and shows preference for SUMO polymers. Here, we further investigate the substrate specificity of SENP6 and show that it is also capable of cleaving mixed chains of SUMO-1 and SUMO-2/3. Depletion of SENP6 results in accumulation of endogenous SUMO-2/3 and S

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Ambaye, Nigus D. "Noncovalent structure of SENP1 in complex with SUMO2." Acta Crystallographica Section F Structural Biology Communications 75, no. 5 (2019): 332–39. http://dx.doi.org/10.1107/s2053230x19004266.

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SUMOylation is a post-translational modification in which a small ubiquitin-like molecule (SUMO) is appended to substrate proteins and is known to influence myriads of biological processes. A delicate interplay between several families of SUMOylation proteins and their substrates ensures the proper level of SUMOylation required for normal cell function. Among the SUMO proteins, SUMO2 is known to form mono-SUMOylated proteins and engage in poly-SUMO chain formation, while sentrin-specific protease 1 (SENP1) is a key enzyme in regulating both events. Determination of the SENP1–SUMO2 interaction

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Zhang, Faying, Hui Zheng, Yufan Xian, et al. "Profiling Substrate Specificity of the SUMO Protease Ulp1 by the YESS–PSSC System to Advance the Conserved Mechanism for Substrate Cleavage." International Journal of Molecular Sciences 23, no. 20 (2022): 12188. http://dx.doi.org/10.3390/ijms232012188.

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SUMO modification is a vital post-translational regulation process in eukaryotes, in which the SUMO protease is responsible for the maturation of the SUMO precursor and the deconjugation of the SUMO protein from modified proteins by accurately cleaving behind the C-terminal Gly–Gly motif. To promote the understanding of the high specificity of the SUMO protease against the SUMO protein as well as to clarify whether the conserved Gly–Gly motif is strictly required for the processing of the SUMO precursor, we systematically profiled the specificity of the S. cerevisiae SUMO protease (Ulp1) on Sm

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Verma, Vivek, Anjil K. Srivastava, Catherine Gough, et al. "SUMO enables substrate selectivity by mitogen-activated protein kinases to regulate immunity in plants." Proceedings of the National Academy of Sciences 118, no. 10 (2021): e2021351118. http://dx.doi.org/10.1073/pnas.2021351118.

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The versatility of mitogen-activated protein kinases (MAPKs) in translating exogenous and endogenous stimuli into appropriate cellular responses depends on its substrate specificity. In animals, several mechanisms have been proposed about how MAPKs maintain specificity to regulate distinct functional pathways. However, little is known of mechanisms that enable substrate selectivity in plant MAPKs. Small ubiquitin-like modifier (SUMO), a posttranslational modification system, plays an important role in plant development and defense by rapid reprogramming of cellular events. In this study we ide

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Li, Shyr-Jiann, and Mark Hochstrasser. "The Ulp1 SUMO isopeptidase." Journal of Cell Biology 160, no. 7 (2003): 1069–82. http://dx.doi.org/10.1083/jcb.200212052.

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Protein modification by the ubiquitin-like SUMO protein contributes to many cellular regulatory mechanisms. In Saccharomyces cerevisiae, both sumoylating and desumoylating activities are essential for viability. Of its two known desumoylating enzymes, Ubl-specific protease (Ulp)1 and Ulp2/Smt4, Ulp1 is specifically required for cell cycle progression. A ∼200-residue segment, the Ulp domain (UD), is conserved among Ulps and includes a core cysteine protease domain that is even more widespread. Here we demonstrate that the Ulp1 UD by itself can support wild-type growth rates and in vitro can cle

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Ji, Mingfei, Zongtao Chai, Jie Chen, et al. "Insights into the Allosteric Effect of SENP1 Q597A Mutation on the Hydrolytic Reaction of SUMO1 via an Integrated Computational Study." Molecules 27, no. 13 (2022): 4149. http://dx.doi.org/10.3390/molecules27134149.

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Small ubiquitin-related modifier (SUMO)-specific protease 1 (SENP1) is a cysteine protease that catalyzes the cleavage of the C-terminus of SUMO1 for the processing of SUMO precursors and deSUMOylation of target proteins. SENP1 is considered to be a promising target for the treatment of hepatocellular carcinoma (HCC) and prostate cancer. SENP1 Gln597 is located at the unstructured loop connecting the helices α4 to α5. The Q597A mutation of SENP1 allosterically disrupts the hydrolytic reaction of SUMO1 through an unknown mechanism. Here, extensive multiple replicates of microsecond molecular dy

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Bea, Annika, Constanze Kröber-Boncardo, Manpreet Sandhu, Christine Brinker, and Joachim Clos. "The Leishmania donovani SENP Protease Is Required for SUMO Processing but Not for Viability." Genes 11, no. 10 (2020): 1198. http://dx.doi.org/10.3390/genes11101198.

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The protozoan parasite Leishmania donovani is part of an early eukaryotic branch and depends on post-transcriptional mechanisms for gene expression regulation. This includes post-transcriptional protein modifications, such as protein phosphorylation. The presence of genes for protein SUMOylation, i.e., the covalent attachment of small ubiquitin-like modifier (SUMO) polypeptides, in the Leishmania genomes prompted us to investigate the importance of the sentrin-specific protease (SENP) and its putative client, SUMO, for the vitality and infectivity of Leishmania donovani. While SENP null mutant

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Smith, Matthew, Vinay Bhaskar, Joseph Fernandez, and Albert J. Courey. "DrosophilaUlp1, a Nuclear Pore-associated SUMO Protease, Prevents Accumulation of Cytoplasmic SUMO Conjugates." Journal of Biological Chemistry 279, no. 42 (2004): 43805–14. http://dx.doi.org/10.1074/jbc.m404942200.

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Malakhov, Michael P., Michael R. Mattern, Oxana A. Malakhova, Mark Drinker, Stephen D. Weeks, and Tauseef R. Butt. "SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins." Journal of Structural and Functional Genomics 5, no. 1/2 (2004): 75–86. http://dx.doi.org/10.1023/b:jsfg.0000029237.70316.52.

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Vethantham, Vasupradha, Nishta Rao, and James L. Manley. "Sumoylation Modulates the Assembly and Activity of the Pre-mRNA 3′ Processing Complex." Molecular and Cellular Biology 27, no. 24 (2007): 8848–58. http://dx.doi.org/10.1128/mcb.01186-07.

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ABSTRACT Eukaryotic pre-mRNA 3′-end formation is catalyzed by a complex set of factors that must be intricately regulated. In this study, we have discovered a novel role for the small ubiquitin-like modifier SUMO in the regulation of mammalian 3′-end processing. We identified symplekin, a factor involved in complex assembly, and CPSF-73, an endonuclease, as SUMO modification substrates. The major sites of sumoylation in symplekin and CPSF-73 were determined and found to be highly conserved across species. A sumoylation-deficient mutant was defective in rescuing cell viability in symplekin smal

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Bailey, Daniel, and Peter O’Hare. "Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease." Journal of General Virology 83, no. 12 (2002): 2951–64. http://dx.doi.org/10.1099/0022-1317-83-12-2951.

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Early during infection, the herpes simplex regulatory protein ICP0 promotes the proteasome-dependent degradation of a number of cellular proteins and the loss of a number of SUMO-1-modified protein isoforms, including PML. Recently, ICP0 has been shown to induce the accumulation of conjugated ubiquitin and function as a ubiquitin E3 ligase. However, certain aspects of the biochemistry, cell biology and the links between SUMO-1 conjugation/deconjugation and protein degradation remain unclear. For example, it is not currently known whether SUMO-1 deconjugation is a prerequisite for ubiquitinatio

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Vera Rodriguez, Arturo, Steffen Frey, and Dirk Görlich. "Engineered SUMO/protease system identifies Pdr6 as a bidirectional nuclear transport receptor." Journal of Cell Biology 218, no. 6 (2019): 2006–20. http://dx.doi.org/10.1083/jcb.201812091.

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Cleavage of affinity tags by specific proteases can be exploited for highly selective affinity chromatography. The SUMO/SENP1 system is the most efficient for such application but fails in eukaryotic expression because it cross-reacts with endogenous proteases. Using a novel selection system, we have evolved the SUMOEu/SENP1Eu pair to orthogonality with the yeast and animal enzymes. SUMOEu fusions therefore remain stable in eukaryotic cells. Likewise, overexpressing a SENP1Eu protease is nontoxic in yeast. We have used the SUMOEu system in an affinity-capture-proteolytic-release approach to id

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Sun, Xiao-Xin, Yingxiao Chen, Yulong Su, et al. "SUMO protease SENP1 deSUMOylates and stabilizes c-Myc." Proceedings of the National Academy of Sciences 115, no. 43 (2018): 10983–88. http://dx.doi.org/10.1073/pnas.1802932115.

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Posttranslational modifications play a crucial role in the proper control of c-Myc protein stability and activity. c-Myc can be modified by small ubiquitin-like modifier (SUMO). However, how SUMOylation regulates c-Myc stability and activity remains to be elucidated. The deSUMOylation enzyme, SENP1, has recently been shown to have a prooncogenic role in cancer; however, mechanistic understanding of this is limited. Here we show that SENP1 is a c-Myc deSUMOylating enzyme. SENP1 interacts with and deSUMOylates c-Myc in cells and in vitro. Overexpression of wild-type SENP1, but not its catalytica

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Lau, Yue-Ting K., Vladimir Baytshtok, Tessa A. Howard, et al. "Discovery and engineering of enhanced SUMO protease enzymes." Journal of Biological Chemistry 293, no. 34 (2018): 13224–33. http://dx.doi.org/10.1074/jbc.ra118.004146.

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Shin, Eun Ju, Hyun Mi Shin, Eori Nam, et al. "DeSUMOylating isopeptidase: a second class of SUMO protease." EMBO reports 13, no. 4 (2012): 339–46. http://dx.doi.org/10.1038/embor.2012.3.

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Mohideen, Firaz, and Christopher D. Lima. "SUMO Takes Control of a Ubiquitin-Specific Protease." Molecular Cell 30, no. 5 (2008): 539–40. http://dx.doi.org/10.1016/j.molcel.2008.05.010.

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Su, Dan, and Mark Hochstrasser. "A WLM Protein with SUMO-Directed Protease Activity." Molecular and Cellular Biology 30, no. 15 (2010): 3734–36. http://dx.doi.org/10.1128/mcb.00673-10.

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Psakhye, Ivan, and Dana Branzei. "SMC complexes are guarded by the SUMO protease Ulp2 against SUMO-chain-mediated turnover." Cell Reports 36, no. 5 (2021): 109485. http://dx.doi.org/10.1016/j.celrep.2021.109485.

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Nishida, Tamotsu, and Yoshiji Yamada. "SMT3IP1, a nucleolar SUMO-specific protease, deconjugates SUMO-2 from nucleolar and cytoplasmic nucleophosmin." Biochemical and Biophysical Research Communications 374, no. 2 (2008): 382–87. http://dx.doi.org/10.1016/j.bbrc.2008.07.047.

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El Mchichi, Bouchra, Tarik Regad, Mohamed-Ali Maroui, et al. "SUMOylation Promotes PML Degradation during Encephalomyocarditis Virus Infection." Journal of Virology 84, no. 22 (2010): 11634–45. http://dx.doi.org/10.1128/jvi.01321-10.

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ABSTRACT The promyelocytic leukemia (PML) protein is expressed in the diffuse nuclear fraction of the nucleoplasm and in matrix-associated structures, known as nuclear bodies (NBs). PML NB formation requires the covalent modification of PML to SUMO. The noncovalent interactions of SUMO with PML based on the identification of a SUMO-interacting motif within PML seem to be required for further recruitment within PML NBs of SUMOylated proteins. RNA viruses whose replication takes place in the cytoplasm and is inhibited by PML have developed various strategies to counteract the antiviral defense m

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Cimarosti, Helena, Emi Ashikaga, Nadia Jaafari, et al. "Enhanced SUMOylation and SENP-1 Protein Levels following Oxygen and Glucose Deprivation in Neurones." Journal of Cerebral Blood Flow & Metabolism 32, no. 1 (2011): 17–22. http://dx.doi.org/10.1038/jcbfm.2011.146.

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Here, we show that oxygen and glucose deprivation (OGD) causes increased small ubiquitin-like modifier (SUMO)-1 and SUMO-2/3 conjugation to substrate proteins in cultured hippocampal neurones. Surprisingly, the SUMO protease SENP-1, which removes SUMO from conjugated proteins, was also increased by OGD, suggesting that the neuronal response to OGD involves a complex interplay between SUMOylation and deSUMOylation. Importantly, decreasing global SUMOylation in cultured hippocampal neurones by overexpression of the catalytic domain of SENP-1 increased neuronal vulnerability to OGD-induced cell d

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Mukhopadhyay, Debaditya, Alexei Arnaoutov, and Mary Dasso. "The SUMO protease SENP6 is essential for inner kinetochore assembly." Journal of Cell Biology 188, no. 5 (2010): 681–92. http://dx.doi.org/10.1083/jcb.200909008.

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We have analyzed the mitotic function of SENP6, a small ubiquitin-like modifier (SUMO) protease that disassembles conjugated SUMO-2/3 chains. Cells lacking SENP6 showed defects in spindle assembly and metaphase chromosome congression. Analysis of kinetochore composition in these cells revealed that a subset of proteins became undetectable on inner kinetochores after SENP6 depletion, particularly the CENP-H/I/K complex, whereas other changes in kinetochore composition mimicked defects previously reported to result from CENP-H/I/K depletion. We further found that CENP-I is degraded through the a

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Colnaghi, Luca, Andrea Conz, Luca Russo, et al. "Neuronal Localization of SENP Proteins with Super Resolution Microscopy." Brain Sciences 10, no. 11 (2020): 778. http://dx.doi.org/10.3390/brainsci10110778.

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SUMOylation of proteins plays a key role in modulating neuronal function. For this reason, the balance between protein SUMOylation and deSUMOylation requires fine regulation to guarantee the homeostasis of neural tissue. While extensive research has been carried out on the localization and function of small ubiquitin-related modifier (SUMO) variants in neurons, less attention has been paid to the SUMO-specific isopeptidases that constitute the human SUMO-specific isopeptidase (SENP)/Ubiquitin-Specific Protease (ULP) cysteine protease family (SENP1-3 and SENP5-7). Here, for the first time, we s

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Xirodimas, Dimitris P., and David P. Lane. "Targeting a nucleolar SUMO protease for degradation: A mechanism by which ARF induces SUMO conjugation." Cell Cycle 7, no. 21 (2008): 3287–91. http://dx.doi.org/10.4161/cc.7.21.7232.

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Best, Jennifer L., Soula Ganiatsas, Sadhana Agarwal, et al. "SUMO-1 Protease-1 Regulates Gene Transcription through PML." Molecular Cell 10, no. 4 (2002): 843–55. http://dx.doi.org/10.1016/s1097-2765(02)00699-8.

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Chung, Sung Soo, Byung Yong Ahn, Min Kim, et al. "Control of Adipogenesis by the SUMO-Specific Protease SENP2." Molecular and Cellular Biology 30, no. 9 (2010): 2135–46. http://dx.doi.org/10.1128/mcb.00852-09.

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ABSTRACT Here, we demonstrate that SENP2, a desumoylating enzyme, plays a critical role in the control of adipogenesis. SENP2 expression was markedly increased upon the induction of adipocyte differentiation, and this increase was dependent on protein kinase A activation. Remarkably, knockdown of SENP2 led to a dramatic attenuation of adipogenesis with a marked decrease in PPARγ and C/EBPα mRNA levels. Knockdown of SENP2 also caused a marked reduction in the level of C/EBPβ protein but not in that of C/EBPβ mRNA. Interestingly, sumoylation of C/EBPβ dramatically increased its ubiquitination an

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