215 results found
    1. Neuroscience

    Identification of a Munc13-sensitive step in chromaffin cell large dense-core vesicle exocytosis

    Kwun Nok M Man et al.
    Munc13 proteins are key determinants of large dense-core vesicle (LDCV)-dependent catecholamine release in chromaffin cells.
    1. Physics of Living Systems

    Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis

    Lu Ma et al.
    The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Autoinhibition of Munc18-1 modulates synaptobrevin binding and helps to enable Munc13-dependent regulation of membrane fusion

    Ewa Sitarska et al.
    Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN

    Junjie Xu et al.
    The crystal structure of a large C-terminal fragment of Munc13-1 provides a key framework to understand how Munc13-1 mediates neurotransmitter release and presynaptic plasticity.
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Membrane bridging by Munc13-1 is crucial for neurotransmitter release

    Bradley Quade et al.
    Cryo-electron tomography, reconstitution, and electrophysiological data show that a fundamental function of Munc13-1 is to bridge synaptic vesicles to the presynaptic plasma membrane.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

    Junyi Jiao et al.
    Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Functional synergy between the Munc13 C-terminal C1 and C2 domains

    Xiaoxia Liu et al.
    Munc13 C-terminal domains synergize to coordinate synaptic vesicle docking, priming and fusion.
    1. Neuroscience

    The active-zone protein Munc13 controls the use-dependence of presynaptic voltage-gated calcium channels

    Nathaniel Calloway et al.
    Munc13, a protein that is essential for exocytosis, controls the behavior of voltage gated calcium channels and shapes synaptic plasticity on fast time scales.
    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

    Munc18-1 is a dynamically regulated PKC target during short-term enhancement of transmitter release

    Özgür Genç et al.
    Protein kinase C brings about post-tetanic potentiation - a temporary increase in synaptic strength due to increased transmitter release - via phosphorylation of a target protein, Munc18-1.

Refine your results by:

Type
Research categories