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Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal

Neuronal porosomes are 15 nm cup-shaped lipoprotein secretory machines composed of nearly 30 proteins present at the presynaptic membrane, that have been investigated using multiple imaging modalities, such as electron microscopy, atomic force microscopy, and solution X-ray. Synaptic vesicles transi...

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Detalles Bibliográficos
Autores principales: Zhvania, Mzia G., Pochkidze, Nino
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Applied Systems srl 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6941571/
https://www.ncbi.nlm.nih.gov/pubmed/32309595
http://dx.doi.org/10.15190/d.2017.7
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author Zhvania, Mzia G.
Pochkidze, Nino
author_facet Zhvania, Mzia G.
Pochkidze, Nino
author_sort Zhvania, Mzia G.
collection PubMed
description Neuronal porosomes are 15 nm cup-shaped lipoprotein secretory machines composed of nearly 30 proteins present at the presynaptic membrane, that have been investigated using multiple imaging modalities, such as electron microscopy, atomic force microscopy, and solution X-ray. Synaptic vesicles transiently dock and fuse at the base of the porosome cup facing the cytosol, by establishing a fusion pore for neurotransmitter release. Studies on the morphology, dynamics, isolation, composition, and reconstitution of the neuronal porosome complex provide a molecular understanding of its structure and function. In the past twenty years, a large body of evidence has accumulated on the involvement of the neuronal porosome proteins in neurotransmission and various neurological disorders. In light of these findings, this review briefly summarizes our current understanding of the neuronal porosome complex, the secretory nanomachine at the nerve terminal.
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spelling pubmed-69415712020-04-17 Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal Zhvania, Mzia G. Pochkidze, Nino Discoveries (Craiova) Focused Review Neuronal porosomes are 15 nm cup-shaped lipoprotein secretory machines composed of nearly 30 proteins present at the presynaptic membrane, that have been investigated using multiple imaging modalities, such as electron microscopy, atomic force microscopy, and solution X-ray. Synaptic vesicles transiently dock and fuse at the base of the porosome cup facing the cytosol, by establishing a fusion pore for neurotransmitter release. Studies on the morphology, dynamics, isolation, composition, and reconstitution of the neuronal porosome complex provide a molecular understanding of its structure and function. In the past twenty years, a large body of evidence has accumulated on the involvement of the neuronal porosome proteins in neurotransmission and various neurological disorders. In light of these findings, this review briefly summarizes our current understanding of the neuronal porosome complex, the secretory nanomachine at the nerve terminal. Applied Systems srl 2017-07-28 /pmc/articles/PMC6941571/ /pubmed/32309595 http://dx.doi.org/10.15190/d.2017.7 Text en Copyright © 2017, Applied Systems http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Focused Review
Zhvania, Mzia G.
Pochkidze, Nino
Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title_full Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title_fullStr Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title_full_unstemmed Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title_short Neuronal Porosome Complex: Secretory Machinery at the Nerve Terminal
title_sort neuronal porosome complex: secretory machinery at the nerve terminal
topic Focused Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6941571/
https://www.ncbi.nlm.nih.gov/pubmed/32309595
http://dx.doi.org/10.15190/d.2017.7
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