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Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions

An action potential triggers neurotransmitter release from synaptic vesicles docking to a specialized release site of the presynaptic plasma membrane, the active zone. The active zone is a highly organized structure with proteins that serves as a platform for synaptic vesicle exocytosis, mediated by...

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Detalles Bibliográficos
Autor principal: Mochida, Sumiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8583982/
https://www.ncbi.nlm.nih.gov/pubmed/34769208
http://dx.doi.org/10.3390/ijms222111775
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author Mochida, Sumiko
author_facet Mochida, Sumiko
author_sort Mochida, Sumiko
collection PubMed
description An action potential triggers neurotransmitter release from synaptic vesicles docking to a specialized release site of the presynaptic plasma membrane, the active zone. The active zone is a highly organized structure with proteins that serves as a platform for synaptic vesicle exocytosis, mediated by SNAREs complex and Ca(2+) sensor proteins, within a sub-millisecond opening of nearby Ca(2+) channels with the membrane depolarization. In response to incoming neuronal signals, each active zone protein plays a role in the release-ready site replenishment with synaptic vesicles for sustainable synaptic transmission. The active zone release apparatus provides a possible link between neuronal activity and plasticity. This review summarizes the mostly physiological role of active zone protein interactions that control synaptic strength, presynaptic short-term plasticity, and homeostatic synaptic plasticity.
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spelling pubmed-85839822021-11-12 Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions Mochida, Sumiko Int J Mol Sci Review An action potential triggers neurotransmitter release from synaptic vesicles docking to a specialized release site of the presynaptic plasma membrane, the active zone. The active zone is a highly organized structure with proteins that serves as a platform for synaptic vesicle exocytosis, mediated by SNAREs complex and Ca(2+) sensor proteins, within a sub-millisecond opening of nearby Ca(2+) channels with the membrane depolarization. In response to incoming neuronal signals, each active zone protein plays a role in the release-ready site replenishment with synaptic vesicles for sustainable synaptic transmission. The active zone release apparatus provides a possible link between neuronal activity and plasticity. This review summarizes the mostly physiological role of active zone protein interactions that control synaptic strength, presynaptic short-term plasticity, and homeostatic synaptic plasticity. MDPI 2021-10-29 /pmc/articles/PMC8583982/ /pubmed/34769208 http://dx.doi.org/10.3390/ijms222111775 Text en © 2021 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Mochida, Sumiko
Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title_full Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title_fullStr Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title_full_unstemmed Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title_short Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions
title_sort stable and flexible synaptic transmission controlled by the active zone protein interactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8583982/
https://www.ncbi.nlm.nih.gov/pubmed/34769208
http://dx.doi.org/10.3390/ijms222111775
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