2024
Balancing acts: The posttranslational modification tightrope of flavivirus replication
Boytz R, Laurent-Rolle M. Balancing acts: The posttranslational modification tightrope of flavivirus replication. PLOS Pathogens 2024, 20: e1012626. PMID: 39466723, PMCID: PMC11516179, DOI: 10.1371/journal.ppat.1012626.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsSUMO-specific protease 1 regulates germinal center B cell response through deSUMOylation of PAX5
Qi J, Yan L, Sun J, Huang C, Su B, Cheng J, Shen L. SUMO-specific protease 1 regulates germinal center B cell response through deSUMOylation of PAX5. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2314619121. PMID: 38776375, PMCID: PMC11145296, DOI: 10.1073/pnas.2314619121.Peer-Reviewed Original ResearchConceptsPaired box protein 5GC B cellsSUMO-specific protease 1Activation-induced cytidine deaminaseProtein SUMOylationClass switch recombinationProtein stabilityB cellsProtease 1B cell responsesProtein 5Cytidine deaminaseSENP1Up-regulatedGC B cell responsesSomatic hypermutationSUMOylationDeSUMOylationGerminal centersHigher affinityProduction of class-switched antibodiesGerminal center B cell responsesGC reactionMemory B cellsClass-switched antibodiesSUMOylation Fine-Tunes Endothelial HEY1 in the Regulation of Angiogenesis
Ren R, Ding S, Ma K, Jiang Y, Wang Y, Chen J, Wang Y, Kou Y, Fan X, Zhu X, Qin L, Qiu C, Simons M, Wei X, Yu L. SUMOylation Fine-Tunes Endothelial HEY1 in the Regulation of Angiogenesis. Circulation Research 2024, 134: 203-222. PMID: 38166414, PMCID: PMC10872267, DOI: 10.1161/circresaha.123.323398.Peer-Reviewed Original ResearchDNA-binding capabilityElectrophoretic mobility shift assaysEndothelial cell-specific expressionMobility shift assaysHairy/EnhancerCell-specific expressionPrimary human endothelial cellsNotch pathway componentsE-box promoter elementsEndothelial cellsRegulation of angiogenesisHelix familyPostnatal vascular growthHey1 functionsTranscriptional complexChromatin immunoprecipitationE3 ligaseRTK signalingEmbryonic developmentMatrigel plug assayPromoter elementsBioinformatics analysisShift assaysSUMOylationDNA binding
2021
RSK1 SUMOylation is required for KSHV lytic replication
Liu Z, Liu C, Wang X, Li W, Zhou J, Dong P, Xiao M, Wang C, Zhang Y, Fu J, Zhu F, Liang Q. RSK1 SUMOylation is required for KSHV lytic replication. PLOS Pathogens 2021, 17: e1010123. PMID: 34871326, PMCID: PMC8675914, DOI: 10.1371/journal.ppat.1010123.Peer-Reviewed Original ResearchConceptsSUMO-interacting motifKSHV lytic replicationKaposi's sarcoma-associated herpesvirusSarcoma-associated herpesvirusEfficient KSHV lytic replicationLytic replicationDownstream substrate phosphorylationAmino acid position 166SUMO-SIM interactionsOverall phosphorylation levelMultiple cellular processesPost-translational modificationsKSHV ORF45Substrate phosphorylationSUMO modificationCellular processesDownstream substratesRSK1 activationDownstream kinasesMAPK pathwaySequence analysisRSK1SUMOylationPhosphorylation levelsPosition 166
2020
Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation
Ryu HY, Zhao D, Li J, Su D, Hochstrasser M. Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation. Nucleic Acids Research 2020, 48: gkaa1093-. PMID: 33231641, PMCID: PMC7708062, DOI: 10.1093/nar/gkaa1093.Peer-Reviewed Original ResearchConceptsHistone deacetylase complexSet3 histone deacetylase complexHistone sumoylationTrans-tail regulationGenome-wide analysisSUMO-interacting motifSUMO conjugation pathwayAltered gene expression profilesDeacetylation of histonesGene expression profilesSet3 complexH2B ubiquitylationDeacetylase complexSpurious transcriptionRNA genesTranscriptional regulationActive genesTranscriptional fidelityTranscription initiationSUMOylationMRNA genesExpression profilesCrosstalk pathwaysHistone deacetylaseGenes
2019
B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis
Li Y, Ma X, Chen Z, Wu H, Wang P, Wu W, Cheng N, Zeng L, Zhang H, Cai X, Chen SJ, Chen Z, Meng G. B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis. Nature Communications 2019, 10: 3789. PMID: 31439836, PMCID: PMC6706441, DOI: 10.1038/s41467-019-11746-0.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinogenesisGene Knockout TechniquesHeLa CellsHumansLeukemia, Promyelocytic, AcuteMiceMice, TransgenicMutationOncogene Proteins, FusionPromyelocytic Leukemia ProteinProtein DomainsProtein MultimerizationRetinoic Acid Receptor alphaScattering, Small AngleSequence Analysis, RNASingle-Cell AnalysisSumoylationX-Ray DiffractionConceptsSingle-cell RNA sequencing analysisRNA sequencing analysisNuclear assemblyPML SUMOylationBiogenesisImportant regulatorOligomerization mechanismSequencing analysisUltracentrifugation analysisOligomerizationPML-RARαTransgenic miceLeukemogenesisGel filtrationSUMOylationSAXS characterizationTransactivationRegulatorProteinMechanismTetramerAssemblyF158Vivo studiesPMLModification of the base excision repair enzyme MBD4 by the small ubiquitin-like molecule SUMO1
Sannai M, Doneddu V, Giri V, Seeholzer S, Nicolas E, Yip S, Bassi M, Mancuso P, Cortellino S, Cigliano A, Lurie R, Ding H, Chernoff J, Sobol R, Yen T, Bagella L, Bellacosa A. Modification of the base excision repair enzyme MBD4 by the small ubiquitin-like molecule SUMO1. DNA Repair 2019, 82: 102687. PMID: 31476572, PMCID: PMC6785017, DOI: 10.1016/j.dnarep.2019.102687.Peer-Reviewed Original ResearchConceptsTandem affinity purificationDNA damage responseSumoylation sitesDamage responseDNA mismatch repair protein MLH1Mismatch repair protein MLH1Main SUMOylation siteCalmodulin affinity columnTranscriptional regulationHEK-293 cellsGenomic stabilityNovel proteinCancer Genome AtlasGlycosylase activitySUMOylationProtein MLH1Affinity purificationMBD4CpG sitesU mismatchesUnmodified speciesRepair activityMissense mutationsGenome AtlasHEK-293
2007
Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation
Hochstrasser M. Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation. 2007, 249-278. DOI: 10.1002/9783527619320.ch11a.Peer-Reviewed Original ResearchSUMO-binding motifMembrane protein traffickingUbiquitin receptorsMVB pathwayUbl conjugationGeneral biochemical functionsBiochemical functionsPositive regulationNegative regulationProtein traffickingProteasome pathwayUbiquitin-like protein conjugationProtein ubiquitinRNA virus buddingCross regulationChange interactionsModification cyclesVirus buddingUbiquitinSulfurtransferasesProteasomeMotifSUMOylationRegulationPathway
2005
Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation
Hochstrasser M. Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation. 2005, 249-278. DOI: 10.1002/9783527620210.ch11.Peer-Reviewed Original ResearchSUMO-binding motifMembrane protein traffickingUbiquitin receptorsMVB pathwayUbl conjugationGeneral biochemical functionsBiochemical functionsPositive regulationNegative regulationProtein traffickingProteasome pathwayUbiquitin-like protein conjugationProtein ubiquitinRNA virus buddingCross regulationChange interactionsModification cyclesVirus buddingUbiquitinSulfurtransferasesProteasomeMotifSUMOylationRegulationPathway
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