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
2018
PRRT2 Regulates Synaptic Fusion by Directly Modulating SNARE Complex Assembly
Coleman J, Jouannot O, Ramakrishnan SK, Zanetti MN, Wang J, Salpietro V, Houlden H, Rothman JE, Krishnakumar SS. PRRT2 Regulates Synaptic Fusion by Directly Modulating SNARE Complex Assembly. Cell Reports 2018, 22: 820-831. PMID: 29346777, PMCID: PMC5792450, DOI: 10.1016/j.celrep.2017.12.056.Peer-Reviewed Original ResearchConceptsProline-rich transmembrane protein 2SNARE complex assemblyComplex assemblyTrans-SNARE complex assemblyTerminal proline-rich domainSynaptic SNARE proteinsProline-rich domainParoxysmal neurological disordersSynaptic vesicle primingLive-cell imagingTransmembrane protein 2Synaptic fusionSNARE proteinsVesicle primingSingle exocytotic eventsBiophysical analysisFusion assaysMolecular mechanismsFunction mutationsPhysiological roleExocytotic eventsPre-synaptic terminalsPC12 cellsProtein 2Single vesicles
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