2025
Correction for Kajaste-Rudnitski et al., “TRIM22 Inhibits HIV-1 Transcription Independently of Its E3 Ubiquitin Ligase Activity, Tat, and NF-κB-Responsive Long Terminal Repeat Elements”
Kajaste-Rudnitski A, Marelli S, Pultrone C, Pertel T, Uchil P, Mechti N, Mothes W, Poli G, Luban J, Vicenzi E. Correction for Kajaste-Rudnitski et al., “TRIM22 Inhibits HIV-1 Transcription Independently of Its E3 Ubiquitin Ligase Activity, Tat, and NF-κB-Responsive Long Terminal Repeat Elements”. Journal Of Virology 2025, 99: e02071-24. PMID: 39868830, PMCID: PMC11853098, DOI: 10.1128/jvi.02071-24.Peer-Reviewed Original Research
2024
Reciprocal antagonism of PIN1-APC/CCDH1 governs mitotic protein stability and cell cycle entry
Ke S, Dang F, Wang L, Chen J, Naik M, Li W, Thavamani A, Kim N, Naik N, Sui H, Tang W, Qiu C, Koikawa K, Batalini F, Stern Gatof E, Isaza D, Patel J, Wang X, Clohessy J, Heng Y, Lahav G, Liu Y, Gray N, Zhou X, Wei W, Wulf G, Lu K. Reciprocal antagonism of PIN1-APC/CCDH1 governs mitotic protein stability and cell cycle entry. Nature Communications 2024, 15: 3220. PMID: 38622115, PMCID: PMC11018817, DOI: 10.1038/s41467-024-47427-w.Peer-Reviewed Original ResearchConceptsCyclin-dependent protein kinasesCell cycle entryMitotic proteinsProtein stabilityActivator of anaphase-promoting complexPermanent cell cycle exitAnaphase-promoting complexE3 ligase activityCo-activator Cdh1Cell cycle exitLigase activityPositive feedback loopProlyl isomerizationProteomic screenProtein kinaseCycle entryProtein turnoverPin1Oncoprotein degradationCo-activationAPC/CCdh1Pin1 inhibitionTriple-negative breast cancerProteinPhosphorylation
2021
The E3 ubiquitin ligase RNF186 and RNF186 risk variants regulate innate receptor-induced outcomes
Ranjan K, Hedl M, Abraham C. The E3 ubiquitin ligase RNF186 and RNF186 risk variants regulate innate receptor-induced outcomes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2013500118. PMID: 34353900, PMCID: PMC8364215, DOI: 10.1073/pnas.2013500118.Peer-Reviewed Original ResearchMeSH KeywordsCytokinesHumansImmunity, InnateInflammatory Bowel DiseasesIntestinesMacrophagesMyeloid CellsNF-kappa BNod2 Signaling Adaptor ProteinPolymorphism, Single NucleotideReceptor-Interacting Protein Serine-Threonine Kinase 2Receptors, Pattern RecognitionToll-Like Receptor 2Toll-Like Receptor 4Ubiquitin-Protein LigasesUbiquitinationConceptsPattern recognition receptorsE3 ubiquitin ligase activityStimulation of PRRsAntimicrobial reactive oxygen speciesMultiple pattern recognition receptorsLoss of functionLigase activityReactive nitrogen speciesComplex assemblyIntestinal myeloid cellsReactive oxygen speciesAutophagy pathwayDownstream signalingRNF186Bacterial clearanceRisk variantsRecognition receptorsHuman macrophagesOxygen speciesInnate immunityInflammatory bowel diseaseNitrogen speciesMicrobial clearanceSpeciesMyeloid cells
2019
GIGANTEA recruits the UBP12 and UBP13 deubiquitylases to regulate accumulation of the ZTL photoreceptor complex
Lee CM, Li MW, Feke A, Liu W, Saffer AM, Gendron JM. GIGANTEA recruits the UBP12 and UBP13 deubiquitylases to regulate accumulation of the ZTL photoreceptor complex. Nature Communications 2019, 10: 3750. PMID: 31434902, PMCID: PMC6704089, DOI: 10.1038/s41467-019-11769-7.Peer-Reviewed Original ResearchConceptsDeubiquitylating enzymesCircadian clockTarget proteinsE3 ubiquitin ligase activityPlant circadian clockUbiquitin-specific protease 12Post-transcriptional mechanismsUbiquitin ligase activityPhotoreceptor complexZTL proteinProtein ubiquitylationInteracting partnerProtein complexesLigase activityZEITLUPEUBP12Gi protein levelsUBP13Enzyme typeLight conditionsGiganteaProtein levelsProteinEnzymeDay light conditions
2016
Novel BET Protein Proteolysis Targeting Chimeras (BETP-PROTACs) Exert Potent Single Agent and Synergistic Activity with Ibrutinib and Venetoclax Against Human Mantle Cell Lymphoma Cells
Sun B, Fiskus W, Zhang L, Raina K, Coleman K, Winkler J, Qian Y, Crew A, Shen A, Saenz D, Mill C, Wang M, Crews C, Bhalla K. Novel BET Protein Proteolysis Targeting Chimeras (BETP-PROTACs) Exert Potent Single Agent and Synergistic Activity with Ibrutinib and Venetoclax Against Human Mantle Cell Lymphoma Cells. Blood 2016, 128: 1058. DOI: 10.1182/blood.v128.22.1058.1058.Peer-Reviewed Original ResearchTarget gene expressionBruton's tyrosine kinaseC-MycARV-825Transcription factorsPrimary MCL cellsTranscriptional activityGene expressionTyrosine kinaseBcl-xLE3 ubiquitin ligase activityMCL cellsUbiquitin ligase activityHuman mantle cell lymphoma cellsB-cell receptor signalingCell receptor signalingBinding of BRD4Regulation of mRNAInk4a/ArfAcetylated chromatinCopy number gainsLigase activityHematopoietic progenitor cellsBET proteinsBETi treatment
2015
Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase
Hudson AM, Mannix KM, Cooley L. Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase. Genetics 2015, 201: 1117-1131. PMID: 26384358, PMCID: PMC4649639, DOI: 10.1534/genetics.115.181289.Peer-Reviewed Original ResearchConceptsKelch functionE3 ligaseCullin-RING E3 ligaseGermline ring canalsActin cytoskeletal organizationDrosophila kelch proteinUbiquitin ligase activityCross-link F-actinUbiquitin E3 ligaseRing canalsKelch proteinProtein substratesCytoskeletal defectsCytoskeletal organizationCytoskeletal remodelingLigase activityCullin 3KelchF-actinCytoskeletonLigaseProteasomeVivoCul3MutagenesisTumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*
Park E, Choi S, Shin B, Yu J, Yu J, Hwang J, Yun H, Chung Y, Choi J, Choi Y, Rho J. Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*. Journal Of Biological Chemistry 2015, 290: 9660-9673. PMID: 25716317, PMCID: PMC4392267, DOI: 10.1074/jbc.m114.609685.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCytokinesGene ExpressionHEK293 CellsHeLa CellsHumansImmunoblottingLysineLysophospholipidsNF-kappa BProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionSphingosineTNF Receptor-Associated Factor 2Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor-alphaUbiquitinUbiquitinationConceptsTRAF-interacting proteinTNFR-associated factor 2TNF-induced inflammatory responseE3 ubiquitin (Ub) ligase activityTNF receptor signaling complexE3 Ub ligasesUbiquitin-dependent pathwayCellular binding partnersMitogen-activated protein kinase activationNF-kB activationNegative regulator of proinflammatory cytokine productionProtein kinase activityDownstream signaling cascadesCell proliferationTNF receptorsUb ligasesTNFR signaling pathwayDown-regulation of proinflammatory cytokine productionLigase activityRING domainTumor necrosis factorProinflammatory cytokine productionAdaptor moleculeCellular processesRegulation of proinflammatory cytokine production
2013
Competing E3 Ubiquitin Ligases Govern Circadian Periodicity by Degradation of CRY in Nucleus and Cytoplasm
Yoo S, Mohawk J, Siepka S, Shan Y, Huh S, Hong H, Kornblum I, Kumar V, Koike N, Xu M, Nussbaum J, Liu X, Chen Z, Chen Z, Green C, Takahashi J. Competing E3 Ubiquitin Ligases Govern Circadian Periodicity by Degradation of CRY in Nucleus and Cytoplasm. Cell 2013, 152: 1091-1105. PMID: 23452855, PMCID: PMC3694781, DOI: 10.1016/j.cell.2013.01.055.Peer-Reviewed Original ResearchConceptsE3 ligase complexLigase complexSCF E3 ligase complexF-box protein genesCircadian periodE3 ligase activityMammalian circadian clockCry proteinsUbiquitin ligasesE3 ligasesCRY degradationLoss of functionCircadian mutantsLigase activityProtein geneCellular compartmentalizationCircadian clockFBXL21FBXL3Missense mutationsLigasesCytoplasmDual roleMutationsTurnover rate
2011
V(D)J Recombination: Mechanisms of Initiation
Schatz DG, Swanson PC. V(D)J Recombination: Mechanisms of Initiation. Annual Review Of Genetics 2011, 45: 167-202. PMID: 21854230, DOI: 10.1146/annurev-genet-110410-132552.Peer-Reviewed Original ResearchConceptsProtein-DNA complexesUbiquitin ligase activityHistone recognitionDomain organizationRAG proteinsRAG2 proteinsLigase activityT-cell receptor genesRecombination signalsDNA breaksHeptamer sequenceLymphocyte developmentDNA breakageDNA cleavageGene segmentsFunctional significanceProper repairReceptor geneRAG1ProteinRecombinationMechanism of initiationComplexesRecent advancesGenes
2001
FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*
Shin M, Ogburn K, Varban O, Gilbert P, Burd C. FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*. Journal Of Biological Chemistry 2001, 276: 41388-41393. PMID: 11526110, DOI: 10.1074/jbc.m105665200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceEndosomesGreen Fluorescent ProteinsIntracellular MembranesLigasesLuminescent ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVacuolesConceptsPI3K productsVacuolar membraneFYVE domainUbiquitin ligaseK productRING-type ubiquitin ligaseUbiquitin ligase activityFYVE fingerFinger motifEukaryotic cellsYeast SaccharomycesCellular proteinsRING domainLigase activityDeletional analysisFusion proteinStructural domainsHistidine residuesPrimary structurePI3KFluorescence microscopyProteinLigaseBindsMembrane
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