235 results found
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Ca2+-dependent release of synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes

    Rashmi Voleti, Klaudia Jaczynska, Josep Rizo
    Ca2+-free synaptotagmin-1 binds to neuronal SNARE complexes anchored on nanodiscs, and Ca2+ releases this interaction to induce tight, specific binding to PIP2-containing membranes.
    1. Computational and Systems Biology
    2. Neuroscience

    Allosteric stabilization of calcium and phosphoinositide dual binding engages several synaptotagmins in fast exocytosis

    Janus RL Kobbersmed, Manon MM Berns ... Alexander M Walter
    A mathematical model of neurotransmitter release predicts that a mutual stabilization of calcium and membrane phospholipids binding to synaptotagmin proteins allows several synaptotagmins to work together for fast synaptic transmission.
    1. Cell Biology
    2. Neuroscience

    Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle replenishment

    Huisheng Liu, Hua Bai ... Edwin R Chapman
    Two proteins—synaptotagmin 7 and calmodulin—have central roles in the calcium-dependent pathway that maintains synaptic transmission.
    1. Neuroscience

    Synaptotagmin-7 places dense-core vesicles at the cell membrane to promote Munc13-2- and Ca2+-dependent priming

    Bassam Tawfik, Joana S Martins ... Jakob Balslev Sørensen
    Synaptotagmin-7 acts synergistically with synaptotagmin-1 by placing vesicles close to the plasma membrane within reach of the SNARE/Munc13-complex, supporting their priming and setting the stage for fast and slow fusion.
    1. Structural Biology and Molecular Biophysics

    All-atom molecular dynamics simulations of Synaptotagmin-SNARE-complexin complexes bridging a vesicle and a flat lipid bilayer

    Josep Rizo, Levent Sari ... Milo M Lin
    Novel insights into the molecular mechanisms underlying neurotransmitter release are provided by all-atom molecular dynamics simulations including SNARE proteins, synaptotagmin-1, complexin-1, a vesicle and a flat bilayer.
    1. Cell Biology
    2. Neuroscience

    Synaptotagmin 1 directs repetitive release by coupling vesicle exocytosis to the Rab3 cycle

    Yunsheng Cheng, Jiaming Wang ... Mei Ding
    Experiments in C. elegans reveal how synaptotagmin and Rab3, the 'yin and yang' of synapses, control whether transmitter vesicles remain docked at the presynaptic membrane or release their contents into the synapse.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    PtdInsP2 and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium

    Ángel Pérez-Lara, Anusa Thapa ... Reinhard Jahn
    Two acidic membrane lipids increase synaptotagmin-1 dwell time and penetration into the membrane, reducing the membrane dissociation of synaptotagmin-1.
    1. Structural Biology and Molecular Biophysics

    Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis

    Sathish Ramakrishnan, Manindra Bera ... Shyam S Krishnakumar
    Cooperative action of synaptotagmin and complexin is needed to arrest all SNARE complexes on a vesicle, and the reversal of the synaptotagmin clamp is sufficient to achieve fast, Ca2+-synchronized fusion.
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Ring-like oligomers of Synaptotagmins and related C2 domain proteins

    Maria N Zanetti, Oscar D Bello ... Shyam S Krishnakumar
    A model for synchronous neurotransmitter release suggests that when not in the presence of calcium ions, Synaptotagmin proteins form ring-like structures between the vesicle and plasma membrane that prevent spontaneous fusion.
    1. Neuroscience
    2. Physics of Living Systems

    The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores

    Zhenyong Wu, Nadiv Dharan ... Erdem Karatekin
    During neurotransmitter release, calcium-induced membrane insertion of the C2B domain of Synaptotagmin re-orients the bound SNARE complex which dilates the fusion pore in a mechanical lever action.

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