2014
Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer
Schauder CM, Wu X, Saheki Y, Narayanaswamy P, Torta F, Wenk MR, De Camilli P, Reinisch KM. Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature 2014, 510: 552-555. PMID: 24847877, PMCID: PMC4135724, DOI: 10.1038/nature13269.Peer-Reviewed Original ResearchDiversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation
Langemeyer L, Bastos R, Cai Y, Itzen A, Reinisch KM, Barr FA. Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation. ELife 2014, 3: e01623. PMID: 24520163, PMCID: PMC3919270, DOI: 10.7554/elife.01623.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAspartic AcidBacterial ProteinsCatalytic DomainDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsEnzyme ActivationGlutamineGuanine Nucleotide Exchange FactorsHeLa CellsHumansHydrolysisListeriaModels, MolecularMutagenesis, Site-DirectedMutationProtein ConformationRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsRab5 GTP-Binding ProteinsSignal TransductionTransfectionConceptsActive site residuesGTP hydrolysis mechanismNucleotide-free formActive site glutamineSwitch II regionDifferent RabsRab activationRab GTPasesGTPase activationGlutamine mutantNucleotide exchangeGDP releaseRabActivation mechanismActivation pathwayActive formPathwayResiduesActivationII regionRAPlasticityGTPasesRab5GEF
2013
The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway
Tan D, Cai Y, Wang J, Zhang J, Menon S, Chou HT, Ferro-Novick S, Reinisch KM, Walz T. The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 19432-19437. PMID: 24218626, PMCID: PMC3845172, DOI: 10.1073/pnas.1316356110.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagyChlorocebus aethiopsChromatography, GelCloning, MolecularCOP-Coated VesiclesCOS CellsElectroporationEscherichia coliImage Processing, Computer-AssistedMicroscopy, ElectronMicroscopy, FluorescenceModels, MolecularProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsConceptsPhagophore assembly siteCOPII vesiclesAssembly sitesRab GTPase Ypt1Electron microscopy structureTargeting of ERTRAPPIII complexFusion machineryMicroscopy structureCOPII coatMacroautophagy pathwayExchange factorSubunit associatesMembrane sourceEM structuresAcceptor compartmentTRAPPIIITRAPPIVesiclesMacroautophagyTrs85COPIISec23Ypt1Mammals
2010
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes
Vasan N, Hutagalung A, Novick P, Reinisch KM. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 14176-14181. PMID: 20660722, PMCID: PMC2922553, DOI: 10.1073/pnas.1009419107.Peer-Reviewed Original ResearchConceptsGolgi-associated retrograde proteinC-terminusC-terminal fragmentGolgi-associated retrograde protein (GARP) complexCommon evolutionary originAlpha-helical bundleTrans-Golgi networkEndosome-derived vesiclesMembrane trafficVesicle recognitionEvolutionary originProtein complexesOligomeric GolgiTerminusSubunitsProteinComplexesDsl1ExocystFragmentsEndosomesGolgiFamilyMutationsVesicles