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Identification of the porosome complex in the hair cell

Porosomes are proposed to be the universal secretory machinery of the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to expel their contents to the extracellular space during cell secretion. In neurons, porosomes are manifested as cup-shaped lipoprotein struc...

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Detalles Bibliográficos
Autores principales: Drescher, Dennis G., Cho, Won Jin, Drescher, Marian J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279744/
https://www.ncbi.nlm.nih.gov/pubmed/22348194
http://dx.doi.org/10.1042/CBR20110005
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author Drescher, Dennis G.
Cho, Won Jin
Drescher, Marian J.
author_facet Drescher, Dennis G.
Cho, Won Jin
Drescher, Marian J.
author_sort Drescher, Dennis G.
collection PubMed
description Porosomes are proposed to be the universal secretory machinery of the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to expel their contents to the extracellular space during cell secretion. In neurons, porosomes are manifested as cup-shaped lipoprotein structures in the presynaptic membrane, 12–17 nm in diameter and possessing a central plug. Hair cells of hearing and balance secrete transmitter from synaptic vesicles in sensory signal transduction, but it has not previously been demonstrated that these mechanosensory cells possess porosome structures that could participate in the secretory process. In the present study, we provide evidence obtained using transmission electron microscopy that porosome structures exist in the hair cell, suggesting a mechanism of hair-cell transmitter secretion markedly different from that of the classic view of the exocytotic process.
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spelling pubmed-32797442012-02-15 Identification of the porosome complex in the hair cell Drescher, Dennis G. Cho, Won Jin Drescher, Marian J. Cell Biol Int Rep (2010) Research Article Porosomes are proposed to be the universal secretory machinery of the cell plasma membrane, where membrane-bound secretory vesicles transiently dock and fuse to expel their contents to the extracellular space during cell secretion. In neurons, porosomes are manifested as cup-shaped lipoprotein structures in the presynaptic membrane, 12–17 nm in diameter and possessing a central plug. Hair cells of hearing and balance secrete transmitter from synaptic vesicles in sensory signal transduction, but it has not previously been demonstrated that these mechanosensory cells possess porosome structures that could participate in the secretory process. In the present study, we provide evidence obtained using transmission electron microscopy that porosome structures exist in the hair cell, suggesting a mechanism of hair-cell transmitter secretion markedly different from that of the classic view of the exocytotic process. Portland Press Ltd 2011-11-15 /pmc/articles/PMC3279744/ /pubmed/22348194 http://dx.doi.org/10.1042/CBR20110005 Text en © The Author(s). http://creativecommons.org/licenses/by-nc/2.5/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commerical use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Drescher, Dennis G.
Cho, Won Jin
Drescher, Marian J.
Identification of the porosome complex in the hair cell
title Identification of the porosome complex in the hair cell
title_full Identification of the porosome complex in the hair cell
title_fullStr Identification of the porosome complex in the hair cell
title_full_unstemmed Identification of the porosome complex in the hair cell
title_short Identification of the porosome complex in the hair cell
title_sort identification of the porosome complex in the hair cell
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279744/
https://www.ncbi.nlm.nih.gov/pubmed/22348194
http://dx.doi.org/10.1042/CBR20110005
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