2015
Phosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity
Cho RW, Buhl LK, Volfson D, Tran A, Li F, Akbergenova Y, Littleton JT. Phosphorylation of Complexin by PKA Regulates Activity-Dependent Spontaneous Neurotransmitter Release and Structural Synaptic Plasticity. Neuron 2015, 88: 749-761. PMID: 26590346, PMCID: PMC4847943, DOI: 10.1016/j.neuron.2015.10.011.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAnimalsBase SequenceCalciumCyclic AMP-Dependent Protein KinasesDrosophilaDrosophila ProteinsExocytosisMolecular Sequence DataNerve Tissue ProteinsNeuromuscular JunctionNeuronal PlasticityNeurotransmitter AgentsPhosphorylationSNARE ProteinsSynaptic TransmissionConceptsSpontaneous neurotransmitter releaseActivity-dependent synaptic growthNeurotransmitter releasePKA-dependent phosphorylationActivity-dependent phosphorylationSynaptic plasticityPresynaptic release machinerySNARE complexRegulated traffickingActivity-dependent mannerC-terminusSynaptic growthSpontaneous releaseStructural synaptic plasticityPhosphorylationStructural plasticityRelease machineryPostsynaptic glutamate receptorsPlasticityNeuronal plasticityGlutamate receptorsSynaptic transmissionNervous systemKey roleFusion mechanism
2011
Complexin cross-links prefusion SNAREs into a zigzag array
Kümmel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM. Complexin cross-links prefusion SNAREs into a zigzag array. Nature Structural & Molecular Biology 2011, 18: 927-933. PMID: 21785414, PMCID: PMC3410656, DOI: 10.1038/nsmb.2101.Peer-Reviewed Original ResearchA 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