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Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1

Neurotransmitter release by Ca(2+)‐triggered synaptic vesicle exocytosis is essential for information transmission in the nervous system. The soluble N‐ethylmaleimide sensitive factor attachment protein receptors (SNAREs) syntaxin‐1, SNAP‐25, and synaptobrevin‐2 form the SNARE complex to bring synap...

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Detalles Bibliográficos
Autores principales: Wang, Shen, Ma, Cong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623535/
https://www.ncbi.nlm.nih.gov/pubmed/35278279
http://dx.doi.org/10.1002/2211-5463.13394
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author Wang, Shen
Ma, Cong
author_facet Wang, Shen
Ma, Cong
author_sort Wang, Shen
collection PubMed
description Neurotransmitter release by Ca(2+)‐triggered synaptic vesicle exocytosis is essential for information transmission in the nervous system. The soluble N‐ethylmaleimide sensitive factor attachment protein receptors (SNAREs) syntaxin‐1, SNAP‐25, and synaptobrevin‐2 form the SNARE complex to bring synaptic vesicles and the plasma membranes together and to catalyze membrane fusion. Munc18‐1 and Munc13‐1 regulate synaptic vesicle priming via orchestrating neuronal SNARE complex assembly. In this review, we summarize recent advances toward the functions and molecular mechanisms of Munc18‐1 and Munc13‐1 in guiding neuronal SNARE complex assembly, and discuss the functional similarities and differences between Munc18‐1 and Munc13‐1 in neurons and their homologs in other intracellular membrane trafficking systems.
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spelling pubmed-96235352022-11-02 Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1 Wang, Shen Ma, Cong FEBS Open Bio Reviews Neurotransmitter release by Ca(2+)‐triggered synaptic vesicle exocytosis is essential for information transmission in the nervous system. The soluble N‐ethylmaleimide sensitive factor attachment protein receptors (SNAREs) syntaxin‐1, SNAP‐25, and synaptobrevin‐2 form the SNARE complex to bring synaptic vesicles and the plasma membranes together and to catalyze membrane fusion. Munc18‐1 and Munc13‐1 regulate synaptic vesicle priming via orchestrating neuronal SNARE complex assembly. In this review, we summarize recent advances toward the functions and molecular mechanisms of Munc18‐1 and Munc13‐1 in guiding neuronal SNARE complex assembly, and discuss the functional similarities and differences between Munc18‐1 and Munc13‐1 in neurons and their homologs in other intracellular membrane trafficking systems. John Wiley and Sons Inc. 2022-03-22 /pmc/articles/PMC9623535/ /pubmed/35278279 http://dx.doi.org/10.1002/2211-5463.13394 Text en © 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Wang, Shen
Ma, Cong
Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title_full Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title_fullStr Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title_full_unstemmed Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title_short Neuronal SNARE complex assembly guided by Munc18‐1 and Munc13‐1
title_sort neuronal snare complex assembly guided by munc18‐1 and munc13‐1
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623535/
https://www.ncbi.nlm.nih.gov/pubmed/35278279
http://dx.doi.org/10.1002/2211-5463.13394
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