2014
Calcium sensitive ring-like oligomers formed by synaptotagmin
Wang J, Bello O, Auclair SM, Wang J, Coleman J, Pincet F, Krishnakumar SS, Sindelar CV, Rothman JE. Calcium sensitive ring-like oligomers formed by synaptotagmin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 13966-13971. PMID: 25201968, PMCID: PMC4183308, DOI: 10.1073/pnas.1415849111.Peer-Reviewed Original ResearchMeSH KeywordsCalciumHumansLipid BilayersMultiprotein ComplexesProtein Structure, TertiarySNARE ProteinsSynaptotagmin IConceptsSynaptic vesicle protein Synaptotagmin 1Cytosolic domainSoluble N-ethylmaleimide-sensitive factorN-ethylmaleimide-sensitive factorMembrane fusion machineryReceptor complex assemblyRing-like oligomersFusion machineryC2 domainComplex assemblySynaptotagmin-1Helical reconstructionFusion proceedsNovel mechanismStructural mechanismsLipid monolayersNeurotransmitter releaseAbsence of calciumPhysiological concentrationsRing formationPresence of calciumFree calcium ionsSynaptotagminCalcium influxCircular arrangementA Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion
Li F, Kümmel D, Coleman J, Reinisch KM, Rothman JE, Pincet F. A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion. Journal Of The American Chemical Society 2014, 136: 3456-3464. PMID: 24533674, PMCID: PMC3985920, DOI: 10.1021/ja410690m.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneKineticsMembrane FusionMiceModels, MolecularProtein Structure, TertiaryRatsSNARE ProteinsThermodynamicsConceptsN-terminal domainMembrane fusionV-SNARET-SNAREsRecent biophysical studiesC-terminal portionSNARE complexTransmembrane domainRegulatory proteinsFunctional intermediatesC-terminusDistinct functionsN-terminusMolecular mechanismsConformational rearrangementsBiophysical studiesVital regulatorZippering mechanismRate-limiting stepBiological membranesSnareFusionComplexinMultiple stagesZippering
2011
A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion
Krishnakumar SS, Radoff DT, Kümmel D, Giraudo CG, Li F, Khandan L, Baguley SW, Coleman J, Reinisch KM, Pincet F, Rothman JE. A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion. Nature Structural & Molecular Biology 2011, 18: 934-940. PMID: 21785412, PMCID: PMC3668341, DOI: 10.1038/nsmb.2103.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayHumansMembrane FusionModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsProtein Structure, TertiaryRatsSynaptosomal-Associated Protein 25SynaptotagminsSyntaxin 1Vesicle-Associated Membrane Protein 2
2008
An Internal Domain of Exo70p Is Required for Actin-independent Localization and Mediates Assembly of Specific Exocyst Components
Hutagalung A, Coleman J, Pypaert M, Novick P. An Internal Domain of Exo70p Is Required for Actin-independent Localization and Mediates Assembly of Specific Exocyst Components. Molecular Biology Of The Cell 2008, 20: 153-163. PMID: 18946089, PMCID: PMC2613103, DOI: 10.1091/mbc.e08-02-0157.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceCell MembraneExocytosisModels, MolecularMolecular Sequence DataMutationProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsRho GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory PathwayVesicular Transport ProteinsConceptsExocyst assemblyPlasma membraneHigh copy number suppressorActin-independent pathwayAmino-terminal domainSynthetic lethal interactionsRod-shaped subunitsNumber suppressorVesicle tethersExocyst componentsExocytic sitesActin cablesExo70pSingle geneSecretory vesiclesLethal interactionsSec3pSynthetic lethalityComplete deletionExocystInternal domainSubunitsDeletionMutationsVesicles