2021
Functional domain studies uncover novel roles for the ZTL Kelch repeat domain in clock function
Feke A, Vanderwall M, Liu W, Gendron JM. Functional domain studies uncover novel roles for the ZTL Kelch repeat domain in clock function. PLOS ONE 2021, 16: e0235938. PMID: 33730063, PMCID: PMC7968664, DOI: 10.1371/journal.pone.0235938.Peer-Reviewed Original ResearchMeSH KeywordsArabidopsisArabidopsis ProteinsChromatography, High Pressure LiquidCircadian ClocksFlowersKelch RepeatMass SpectrometryPeptidesPhenotypePlants, Genetically ModifiedConceptsLOV KELCH PROTEIN 2Kelch repeat domainRepeat domainLOV domainsF-BOX PROTEIN 1Protein-protein interaction domainsPlant circadian clockFLAVIN-BINDING KELCHProtein domain architecturePotential interacting partnerE3 ubiquitin ligasesInteracting partnerDomain architectureProtein complexesUbiquitin ligasesKelch proteinProtein familyTransgenic linesFlowering timeKelch familyProtein domainsZEITLUPEInteraction domainClock functionUnique photoreceptor
2019
Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function
Feke A, Liu W, Hong J, Li MW, Lee CM, Zhou EK, Gendron JM. Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function. ELife 2019, 8: e44558. PMID: 30950791, PMCID: PMC6483598, DOI: 10.7554/elife.44558.Peer-Reviewed Original ResearchConceptsE3 ubiquitin ligasesUbiquitin ligasesCircadian clockCircadian functionPlant E3 ubiquitin ligasesTransgenic Arabidopsis plantsNew potential regulatorsArabidopsis plantsRegulated degradationPlant developmentClock proteinsClock regulatorsFunctional redundancyE3 ubiquitinProtein degradationGenetic challengesLigasesPotential regulatorCircadian periodScreening platformUbiquitinRegulatorDecoysSplicingClock
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 ResearchMeSH KeywordsArabidopsisArabidopsis ProteinsCircadian ClocksFlowersGene Expression Regulation, PlantPlants, Genetically ModifiedProtein DomainsProtein Interaction MapsRepressor ProteinsUbiquitinationConceptsLOV 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
2011
PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1
Tang W, Yuan M, Wang R, Yang Y, Wang C, Oses-Prieto JA, Kim TW, Zhou HW, Deng Z, Gampala SS, Gendron JM, Jonassen EM, Lillo C, DeLong A, Burlingame AL, Sun Y, Wang ZY. PP2A activates brassinosteroid-responsive gene expression and plant growth by dephosphorylating BZR1. Nature Cell Biology 2011, 13: 124-131. PMID: 21258370, PMCID: PMC3077550, DOI: 10.1038/ncb2151.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArabidopsisArabidopsis ProteinsDNA-Binding ProteinsGene Expression Regulation, PlantMolecular Sequence DataNuclear ProteinsPhosphorylationPlant Growth RegulatorsPlants, Genetically ModifiedProtein Phosphatase 2Sequence AlignmentSignal TransductionTriazolesTwo-Hybrid System Techniques
2007
A Proteomics Study of Brassinosteroid Response in Arabidopsis *
Deng Z, Zhang X, Tang W, Oses-Prieto JA, Suzuki N, Gendron JM, Chen H, Guan S, Chalkley RJ, Peterman TK, Burlingame AL, Wang ZY. A Proteomics Study of Brassinosteroid Response in Arabidopsis *. Molecular & Cellular Proteomics 2007, 6: 2058-2071. PMID: 17848588, PMCID: PMC2966871, DOI: 10.1074/mcp.m700123-mcp200.Peer-Reviewed Original ResearchMeSH KeywordsArabidopsisBase SequenceChromatography, LiquidDNA PrimersElectrophoresis, Gel, Two-DimensionalPhosphorylationPlants, Genetically ModifiedProteomicsSteroidsTandem Mass SpectrometryConceptsTwo-dimensional DIGEProteomic studiesBiosynthesis of hormonesSpecific cellular processesPrevious microarray studyBri1-116Bzr1-1DBrassinosteroid responsesBR regulationBR actionVesicle traffickingBR responsesCellular processesRT-PCR analysisPosttranslational modificationsBrassinosteroidsCytoskeleton rearrangementMolecular detailsProtein responseBR treatmentPlant steroidsBR mutantsMolecular networksDiverse processesPhysiological processes
2005
BZR1 Is a Transcriptional Repressor with Dual Roles in Brassinosteroid Homeostasis and Growth Responses
He JX, Gendron JM, Sun Y, Gampala SS, Gendron N, Sun CQ, Wang ZY. BZR1 Is a Transcriptional Repressor with Dual Roles in Brassinosteroid Homeostasis and Growth Responses. Science 2005, 307: 1634-1638. PMID: 15681342, PMCID: PMC2925132, DOI: 10.1126/science.1107580.Peer-Reviewed Original ResearchMeSH KeywordsArabidopsisArabidopsis ProteinsBase SequenceBinding SitesChromatin ImmunoprecipitationDNA-Binding ProteinsFeedback, PhysiologicalGene Expression Regulation, PlantGenes, PlantGenes, ReporterHomeostasisLightMutationNuclear ProteinsOligonucleotide Array Sequence AnalysisPhenotypePlant Growth RegulatorsPlants, Genetically ModifiedPromoter Regions, GeneticRecombinant Fusion ProteinsRepressor ProteinsSignal TransductionSteroidsTranscription, GeneticConceptsBrassinosteroid homeostasisTranscriptional repressorCell surface receptor kinaseBR biosynthetic genesDevelopment of plantsGrowth responseBR homeostasisBR biosynthesisBiosynthetic genesBZR1Dual roleReceptor kinaseAdditional potential targetsGene expressionMicroarray analysisUnknown DNARepressorNormal growthHomeostasisPotential targetPhysiological studiesDephosphorylationBiosynthesisKinaseGenes
2002
The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis
He JX, Gendron JM, Yang Y, Li J, Wang ZY. The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 10185-10190. PMID: 12114546, PMCID: PMC126645, DOI: 10.1073/pnas.152342599.Peer-Reviewed Original ResearchMeSH KeywordsArabidopsisArabidopsis ProteinsCalcium-Calmodulin-Dependent Protein KinasesDNA-Binding ProteinsGene Expression Regulation, PlantGlycogen Synthase Kinase 3Glycogen Synthase KinasesGreen Fluorescent ProteinsLuminescent ProteinsNuclear ProteinsPhosphorylationPhytosterolsPlants, Genetically ModifiedProtein KinasesSignal TransductionConceptsPositive regulatorBZR2/BES1Two-hybrid assayBZR1 proteinReceptor BRI1BZR1Proteasome machineryBrassinosteroidsBIN2 activityNegative regulatorBIN2Protein accumulationRegulatorNormal growthDephosphorylationProteasome inhibitorsAccumulationBES1BRI1ArabidopsisPhosphorylatesSteroid hormonesMG132YeastPhosphorylation