111 results found
    1. Cell Biology
    2. Neuroscience

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

    Yunsheng Cheng et al.
    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. Cell Biology
    2. Neuroscience

    The postsynaptic t-SNARE Syntaxin 4 controls traffic of Neuroligin 1 and Synaptotagmin 4 to regulate retrograde signaling

    Kathryn P Harris et al.
    Syntaxin 4 regulates retrograde signaling in the postsynaptic compartment at Drosophila synapses by controlling trafficking of Neuroligin and Synaptotagmin 4 cargo.
    1. Cell Biology
    2. Neuroscience

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

    Huisheng Liu et al.
    Two proteins—synaptotagmin 7 and calmodulin—have central roles in the calcium-dependent pathway that maintains synaptic transmission.
    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 et al.
    Two acidic membrane lipids increase synaptotagmin-1 dwell time and penetration into the membrane, reducing the membrane dissociation of synaptotagmin-1.
    1. Neuroscience

    A synaptotagmin suppressor screen indicates SNARE binding controls the timing and Ca2+ cooperativity of vesicle fusion

    Zhuo Guan et al.
    A suppressor screen of dominant-negative synaptotagmin-induced lethality in Drosophila identifies key properties of the protein that regulate fusion, including the SNARE interaction surface.
    1. Neuroscience

    Doc2B acts as a calcium sensor for vesicle priming requiring synaptotagmin-1, Munc13-2 and SNAREs

    Sébastien Houy et al.
    Doc2B functions in two distinct vesicle priming steps; membrane localization occludes upstream Ca2+-dependent priming, whereas Ca2+-binding and interaction with synaptotagmin-1, SNAREs, and Munc13-2 are involved in downstream priming, which makes vesicles readily releasable.
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Ring-like oligomers of Synaptotagmins and related C2 domain proteins

    Maria N Zanetti et al.
    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

    Circular oligomerization is an intrinsic property of synaptotagmin

    Jing Wang et al.
    Calcium-binding synaptotagmins are involved in ring oligomer formation, which allows synaptotagmins to synchronize neurotransmitter release to Ca2+ influx.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Synaptotagmin-1 C2B domain interacts simultaneously with SNAREs and membranes to promote membrane fusion

    Shen Wang et al.
    When the Ca2+-binding loops of the C2B domain insert into a membrane, interactions with a phospholipid and the SNARE complex allow synaptotagmin-1 to bend the membrane.
    1. Cell Biology
    2. Neuroscience

    Phosphatidylinositol 4,5-bisphosphate optical uncaging potentiates exocytosis

    Alexander M Walter et al.
    Increasing PI(4,5)P2 on a sub-second timescale using a novel, membrane-permeant UV activatable PI(4,5)P2 molecule augments exocytosis which requires the PI(4,5)P2 interacting exocytotic proteins Munc13-2 and synaptotagmin-1.

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