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
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