2023
HEXOKINASE1 and glucose-6-phosphate fuel plant growth and development
Vanderwall M, Gendron J. HEXOKINASE1 and glucose-6-phosphate fuel plant growth and development. Development 2023, 150 PMID: 37842778, PMCID: PMC10617624, DOI: 10.1242/dev.202346.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsCatalytic functionPlant metabolic pathwaysEnzyme catalytic functionPlant developmentPhotoautotrophic organismsGlucose-6-phosphate productionHexokinase1Plant growthPhosphorylation of hexosesBiosynthetic routeMetabolic enzymesMetabolic pathwaysPlantsDevelopmental significancePathwayPhosphorylationOrganismsEnzymeMetabolismPigmentsPrevious studiesHexosesDiscrete areasCatalytic activityFunction
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
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 ResearchConceptsTwo-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 processesAn Essential Role for 14-3-3 Proteins in Brassinosteroid Signal Transduction in Arabidopsis
Gampala SS, Kim TW, He JX, Tang W, Deng Z, Bai MY, Guan S, Lalonde S, Sun Y, Gendron JM, Chen H, Shibagaki N, Ferl RJ, Ehrhardt D, Chong K, Burlingame AL, Wang ZY. An Essential Role for 14-3-3 Proteins in Brassinosteroid Signal Transduction in Arabidopsis. Developmental Cell 2007, 13: 177-189. PMID: 17681130, PMCID: PMC2000337, DOI: 10.1016/j.devcel.2007.06.009.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAmino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCell NucleusDNA, PlantDNA-Binding ProteinsDown-RegulationModels, BiologicalMolecular Sequence DataMutationNuclear ProteinsPhosphorylationPlant LeavesProtein BindingProtein KinasesProtein TransportSignal TransductionSteroids, HeterocyclicConceptsPlant growthTranscription factorsNuclear localizationGene expressionBZR2/BES1Brassinosteroid signal transductionSignal transduction pathwaysKey transcription factorRapid nuclear localizationBZR1 proteinCell surface receptorsBR regulationBR deficiencyTransgenic plantsGSK3 kinaseBR responsesCytoplasmic retentionSignal transductionTransduction pathwaysCytoplasmic localizationDNA bindingBrassinosteroidsBR treatmentBZR1Essential hormone
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