2021
Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis
Sepulveda-Garcia E, Fulton EC, Parlan EV, O’Connor L, Fleming AA, Replogle AJ, Rocha-Sosa M, Gendron JM, Thines B. Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis. Plants 2021, 10: 2228. PMID: 34686037, PMCID: PMC8537223, DOI: 10.3390/plants10102228.Peer-Reviewed Original ResearchFBX proteinsSCF complexSCF-type E3 ubiquitin ligasesProtein targetsF-box domainF-box proteinsProtein degradation eventsE3 ubiquitin ligasesFBS proteinsC-terminal domainSkp proteinInteracting proteinSubstrate adaptorUbiquitin ligasesDomain interactsEnvironmental stressBiological functionsC-terminusN-terminusFacilitate recruitmentProtein pathwayFB proteinNuclear eventsArabidopsisProtein
2020
A Decoy Library Uncovers U-Box E3 Ubiquitin Ligases That Regulate Flowering Time in Arabidopsis
Feke AM, Hong J, Liu W, Gendron JM. A Decoy Library Uncovers U-Box E3 Ubiquitin Ligases That Regulate Flowering Time in Arabidopsis. Genetics 2020, 215: 699-712. PMID: 32434795, PMCID: PMC7337086, DOI: 10.1534/genetics.120.303199.Peer-Reviewed Original ResearchConceptsE3 ubiquitin ligasesUbiquitin ligasesU-box E3 ubiquitin ligasesReproductive developmentReverse genetic screenMOS4-associated complexDominant-negative strategyGenetic redundancyGenetic screenTransgenic populationsTargeted degradationLigasesUnidentified regulatorDevelopmental transitionsBiological processesGenetic characterizationU-boxBiochemical studiesWidespread importanceRegulatorArabidopsisOrganismsPlantsProteinComplexes
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
2018
Decoys Untangle Complicated Redundancy and Reveal Targets of Circadian Clock F-Box Proteins
Lee CM, Feke A, Li MW, Adamchek C, Webb K, Pruneda-Paz J, Bennett EJ, Kay SA, Gendron JM. Decoys Untangle Complicated Redundancy and Reveal Targets of Circadian Clock F-Box Proteins. Plant Physiology 2018, 177: 1170-1186. PMID: 29794020, PMCID: PMC6052990, DOI: 10.1104/pp.18.00331.Peer-Reviewed Original ResearchConceptsLOV KELCH PROTEIN2Target proteinsCircadian clockEukaryotic circadian clocksF-box proteinsE3 ubiquitin ligasesUbiquitin-proteasome systemDominant-negative formImmunoprecipitation-mass spectrometryMutant plantsF-BOX1Genetic redundancyChe proteinsKELCH REPEATClock proteinsUbiquitin ligasesZEITLUPEFlowering timeFKF1Proteasome systemFlavin bindingBiochemical roleProteinLight conditionsUbiquitylation
2017
Mapping Protein–Protein Interactions Using Affinity Purification and Mass Spectrometry
Lee CM, Adamchek C, Feke A, Nusinow DA, Gendron JM. Mapping Protein–Protein Interactions Using Affinity Purification and Mass Spectrometry. Methods In Molecular Biology 2017, 1610: 231-249. PMID: 28439867, DOI: 10.1007/978-1-4939-7003-2_15.Peer-Reviewed Original ResearchConceptsAP-MSHigher-order protein complexesAffinity purificationMapping protein-protein interactionsProtein-protein interaction networkProtein-protein interactionsMeaningful complexesProtein interactomeProtein complexesProtein-specific antibodiesMass spectrometry technologyInteraction networksCellular pathwaysTransient interactionsMass spectrometryInteractomeNonspecific interactionsSpectrometry technologyUnbiased methodComplexesPurificationComprehensive knowledgeCrucial stepPlantsProtein
2015
The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins
Higgins R, Gendron JM, Rising L, Mak R, Webb K, Kaiser SE, Zuzow N, Riviere P, Yang B, Fenech E, Tang X, Lindsay SA, Christianson JC, Hampton RY, Wasserman SA, Bennett EJ. The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins. Molecular Cell 2015, 59: 35-49. PMID: 26051182, PMCID: PMC4491043, DOI: 10.1016/j.molcel.2015.04.026.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell SurvivalDrosophilaEIF-2 KinaseEndoplasmic ReticulumEndoplasmic Reticulum StressEukaryotic Initiation Factor-2Gene Expression RegulationHumansMolecular Sequence DataPhosphorylationProtein BiosynthesisRibosome Subunits, Small, EukaryoticSaccharomyces cerevisiaeUbiquitinationUnfolded Protein ResponseConceptsUnfolded protein responseRegulatory ubiquitylationRibosomal proteinsUPR activationEukaryotic translational controlUbiquitin-dependent regulationER-resident proteinsChronic UPR activationTranslational reprogrammingER homeostasisTranslational controlCytoplasmic ribosomesProtein foldingTranslation inhibitionProtein responseUbiquitylationPERK signalingUbiquitin proteomicsOptimal cell survivalCell survivalProtein synthesisProteinDegradation capacityReprogrammingActivation
2014
Using the ubiquitin‐modified proteome to monitor protein synthesis fidelity (353.1)
Bennett E, Webb K, Zuzow N, Gendron J. Using the ubiquitin‐modified proteome to monitor protein synthesis fidelity (353.1). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.353.1.Peer-Reviewed Original ResearchUbiquitin-modified proteomeUPS-dependent degradationUbiquitin-dependent destructionUbiquitylation eventsUbiquitylation substratesUbiquitylated proteinsProtein translationTranslation productsProteomic techniquesDeleterious accumulationLysine residuesHomeostasis functionsProteinDefense strategiesImmunoaffinity methodProteomeLarge poolTrypsinolysisResiduesPrevious studiesAccumulationPoolPeptides
2009
Exploring the transcriptional landscape of plant circadian rhythms using genome tiling arrays
Hazen SP, Naef F, Quisel T, Gendron JM, Chen H, Ecker JR, Borevitz JO, Kay SA. Exploring the transcriptional landscape of plant circadian rhythms using genome tiling arrays. Genome Biology 2009, 10: r17. PMID: 19210792, PMCID: PMC2688271, DOI: 10.1186/gb-2009-10-2-r17.Peer-Reviewed Original ResearchConceptsArabidopsis genomeCircadian clockCircadian clock regulationPlant circadian rhythmsSmall nucleolar RNAsGenome tiling arraysRhythmic expression patternCircadian rhythmClock regulationTranscriptional landscapeTiling arraysIntergenic regionNucleolar RNAsAntisense transcriptsUnbiased interrogationWhole genomeNoncoding regionsExpression patternsGenomeSense strandTranscriptsGenesProteinUnbiased analysisIntrons
2007
Multiple mechanisms modulate brassinosteroid signaling
Gendron JM, Wang ZY. Multiple mechanisms modulate brassinosteroid signaling. Current Opinion In Plant Biology 2007, 10: 436-441. PMID: 17904409, PMCID: PMC2093957, DOI: 10.1016/j.pbi.2007.08.015.Peer-Reviewed Original ResearchConceptsTranscription factorsCell surface receptor kinaseSubsequent biochemical studiesBR perceptionNuclear transcription factorPlant growthMultiple mechanismsReceptor kinaseGene expressionIntracellular kinasesGenetic studiesBiochemical studiesCell surfaceEssential hormoneKinasePathwayRecent studiesBRI1BAK1BrassinosteroidsEndosomesMajor gapsPhosphorylationKey componentProtein