2020
Munc13 binds and recruits SNAP25 to chaperone SNARE complex assembly
Sundaram R, Jin H, Li F, Shu T, Coleman J, Yang J, Pincet F, Zhang Y, Rothman JE, Krishnakumar SS. Munc13 binds and recruits SNAP25 to chaperone SNARE complex assembly. FEBS Letters 2020, 595: 297-309. PMID: 33222163, PMCID: PMC8068094, DOI: 10.1002/1873-3468.14006.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsLipid BilayersLiposomesMiceModels, MolecularNerve Tissue ProteinsOptical TweezersPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylserinesPolyethylene GlycolsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsRecombinant Fusion ProteinsSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2ConceptsSNARE complex assemblyComplex assemblyMunc13-1 MUN domainDetailed structure-function analysisSNARE protein VAMP2Syntaxin 1/Structure-function analysisSynaptic vesicle fusionOptical tweezers studiesSNARE assemblySNARE motifMUN domainMunc18-1Syntaxin-1Munc13-1FRET spectroscopyLinker regionVesicle fusionDirect bindingPhospholipid bilayersPresynaptic membraneSNAP25AssemblyBindingRecruits
2019
Structural basis for the clamping and Ca2+ activation of SNARE-mediated fusion by synaptotagmin
Grushin K, Wang J, Coleman J, Rothman JE, Sindelar CV, Krishnakumar SS. Structural basis for the clamping and Ca2+ activation of SNARE-mediated fusion by synaptotagmin. Nature Communications 2019, 10: 2413. PMID: 31160571, PMCID: PMC6546687, DOI: 10.1038/s41467-019-10391-x.Peer-Reviewed Original ResearchConceptsCryo-electron microscopy structureActivation of SNAREsDependent membrane interactionsAnionic lipid headgroupsFusion clampActivator functionSNARE bundleSNARE proteinsMicroscopy structureC2B domainStructural basisSynaptotagmin-1SNAREpinsAliphatic loopsMembrane interactionsComplete assemblyLipid headgroupsLipid membranesNeurotransmitter releaseMembraneKey determinantSynaptotagminSyt1Calcium influxPartial insertion
2018
Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis
Bello OD, Jouannot O, Chaudhuri A, Stroeva E, Coleman J, Volynski KE, Rothman JE, Krishnakumar SS. Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e7624-e7631. PMID: 30038018, PMCID: PMC6094142, DOI: 10.1073/pnas.1808792115.Peer-Reviewed Original ResearchConceptsRegulated exocytosisFusion machineryC2 domain proteinsCore fusion machinerySingle vesicle exocytosisConstitutive exocytosisPrincipal CaVesicular releaseMolecular mechanismsSensitive oligomersExocytosisPheochromocytoma cellsSelective disruptionSpontaneous fusionCritical roleMachineryOligomerizationDirect activationCentral componentStructural featuresConsiderable insightCalcium controlPHluorinSyt1SYTRearrangements under confinement lead to increased binding energy of Synaptotagmin‐1 with anionic membranes in Mg2+ and Ca2+
Gruget C, Coleman J, Bello O, Krishnakumar SS, Perez E, Rothman JE, Pincet F, Donaldson SH. Rearrangements under confinement lead to increased binding energy of Synaptotagmin‐1 with anionic membranes in Mg2+ and Ca2+. FEBS Letters 2018, 592: 1497-1506. PMID: 29578584, DOI: 10.1002/1873-3468.13040.Peer-Reviewed Original ResearchMeSH KeywordsCalciumCell MembraneDose-Response Relationship, DrugMagnesiumProtein BindingSurface PropertiesSynaptotagmin IThermodynamics
2016
Ring-like oligomers of Synaptotagmins and related C2 domain proteins
Zanetti MN, Bello OD, Wang J, Coleman J, Cai Y, Sindelar CV, Rothman JE, Krishnakumar SS. Ring-like oligomers of Synaptotagmins and related C2 domain proteins. ELife 2016, 5: e17262. PMID: 27434670, PMCID: PMC4977156, DOI: 10.7554/elife.17262.Peer-Reviewed Original Research
2015
Re-visiting the trans insertion model for complexin clamping
Krishnakumar SS, Li F, Coleman J, Schauder CM, Kümmel D, Pincet F, Rothman JE, Reinisch KM. Re-visiting the trans insertion model for complexin clamping. ELife 2015, 4: e04463. PMID: 25831964, PMCID: PMC4384536, DOI: 10.7554/elife.04463.Peer-Reviewed Original ResearchAdaptor Proteins, Vesicular TransportAlgorithmsAnimalsCalorimetryCircular DichroismEntropyFluorescence Resonance Energy TransferHumansKineticsMembrane FusionModels, NeurologicalMutationNerve Tissue ProteinsNeuronsProtein BindingSignal TransductionSNARE ProteinsSynaptic TransmissionSynaptotagminsVesicle-Associated Membrane Protein 2
2013
FisB mediates membrane fission during sporulation in Bacillus subtilis
Doan T, Coleman J, Marquis KA, Meeske AJ, Burton BM, Karatekin E, Rudner DZ. FisB mediates membrane fission during sporulation in Bacillus subtilis. Genes & Development 2013, 27: 322-334. PMID: 23388828, PMCID: PMC3576517, DOI: 10.1101/gad.209049.112.Peer-Reviewed Original ResearchConceptsMother cell membraneMembrane fissionPhagocytic-like processBacillus subtilisLarger mother cellProkaryotic cell biologyMother cell cytoplasmCell membraneSmaller foresporeSite of fissionFission machineryMembrane topologyMembrane remodelingExtracytoplasmic domainMother cellsFission proteinsSpore formationCell biologySporulating cellsForesporeFisBCell cytoplasmRemarkable specificityOutstanding questionsSubtilis
2011
Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex
Shi L, Kümmel D, Coleman J, Melia TJ, Giraudo CG. Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex. Molecular Biology Of The Cell 2011, 22: 4150-4160. PMID: 21900493, PMCID: PMC3204075, DOI: 10.1091/mbc.e11-02-0150.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalorimetryCell MembraneHeLa CellsHuman Growth HormoneHumansLiposomesMiceMicroscopy, FluorescenceMolecular ChaperonesMunc18 ProteinsNeuroendocrine CellsPC12 CellsProtein BindingProtein Interaction Domains and MotifsProtein TransportRatsRecombinant ProteinsSNARE ProteinsSyntaxin 1ThermodynamicsTitrimetryConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSyntaxin 1AMunc18-1N-ethylmaleimide-sensitive factor attachment protein receptorsSec1/Munc18 (SM) proteinsFactor attachment protein receptorsCentral cavitySNARE complex assemblyIntracellular membrane traffickingAttachment protein receptorsMunc18-1 mutantsLiposome fusionPrecise molecular mechanismsMunc18 proteinsMembrane traffickingSNARE complexChaperone functionH3 domainDistinct binding modesMembrane fusionMolecular mechanismsProtein receptorsDual functionNeuroendocrine cellsBinding modes