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Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells

Over the past years, dynamin has been implicated in tuning the amount and nature of transmitter released during exocytosis. However, the mechanism involved remains poorly understood. Here, using bovine adrenal chromaffin cells, we investigated whether this mechanism rely on dynamin’s ability to remo...

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Autores principales: González-Jamett, Arlek M., Momboisse, Fanny, Guerra, María José, Ory, Stéphane, Báez-Matus, Ximena, Barraza, Natalia, Calco, Valerie, Houy, Sébastien, Couve, Eduardo, Neely, Alan, Martínez, Agustín D., Gasman, Stéphane, Cárdenas, Ana M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3734226/
https://www.ncbi.nlm.nih.gov/pubmed/23940613
http://dx.doi.org/10.1371/journal.pone.0070638
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author González-Jamett, Arlek M.
Momboisse, Fanny
Guerra, María José
Ory, Stéphane
Báez-Matus, Ximena
Barraza, Natalia
Calco, Valerie
Houy, Sébastien
Couve, Eduardo
Neely, Alan
Martínez, Agustín D.
Gasman, Stéphane
Cárdenas, Ana M.
author_facet González-Jamett, Arlek M.
Momboisse, Fanny
Guerra, María José
Ory, Stéphane
Báez-Matus, Ximena
Barraza, Natalia
Calco, Valerie
Houy, Sébastien
Couve, Eduardo
Neely, Alan
Martínez, Agustín D.
Gasman, Stéphane
Cárdenas, Ana M.
author_sort González-Jamett, Arlek M.
collection PubMed
description Over the past years, dynamin has been implicated in tuning the amount and nature of transmitter released during exocytosis. However, the mechanism involved remains poorly understood. Here, using bovine adrenal chromaffin cells, we investigated whether this mechanism rely on dynamin’s ability to remodel actin cytoskeleton. According to this idea, inhibition of dynamin GTPase activity suppressed the calcium-dependent de novo cortical actin and altered the cortical actin network. Similarly, expression of a small interfering RNA directed against dynamin-2, an isoform highly expressed in chromaffin cells, changed the cortical actin network pattern. Disruption of dynamin-2 function, as well as the pharmacological inhibition of actin polymerization with cytochalasine-D, slowed down fusion pore expansion and increased the quantal size of individual exocytotic events. The effects of cytochalasine-D and dynamin-2 disruption were not additive indicating that dynamin-2 and F-actin regulate the late steps of exocytosis by a common mechanism. Together our data support a model in which dynamin-2 directs actin polymerization at the exocytosis site where both, in concert, adjust the hormone quantal release to efficiently respond to physiological demands.
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spelling pubmed-37342262013-08-12 Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells González-Jamett, Arlek M. Momboisse, Fanny Guerra, María José Ory, Stéphane Báez-Matus, Ximena Barraza, Natalia Calco, Valerie Houy, Sébastien Couve, Eduardo Neely, Alan Martínez, Agustín D. Gasman, Stéphane Cárdenas, Ana M. PLoS One Research Article Over the past years, dynamin has been implicated in tuning the amount and nature of transmitter released during exocytosis. However, the mechanism involved remains poorly understood. Here, using bovine adrenal chromaffin cells, we investigated whether this mechanism rely on dynamin’s ability to remodel actin cytoskeleton. According to this idea, inhibition of dynamin GTPase activity suppressed the calcium-dependent de novo cortical actin and altered the cortical actin network. Similarly, expression of a small interfering RNA directed against dynamin-2, an isoform highly expressed in chromaffin cells, changed the cortical actin network pattern. Disruption of dynamin-2 function, as well as the pharmacological inhibition of actin polymerization with cytochalasine-D, slowed down fusion pore expansion and increased the quantal size of individual exocytotic events. The effects of cytochalasine-D and dynamin-2 disruption were not additive indicating that dynamin-2 and F-actin regulate the late steps of exocytosis by a common mechanism. Together our data support a model in which dynamin-2 directs actin polymerization at the exocytosis site where both, in concert, adjust the hormone quantal release to efficiently respond to physiological demands. Public Library of Science 2013-08-05 /pmc/articles/PMC3734226/ /pubmed/23940613 http://dx.doi.org/10.1371/journal.pone.0070638 Text en © 2013 González-Jamett et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
González-Jamett, Arlek M.
Momboisse, Fanny
Guerra, María José
Ory, Stéphane
Báez-Matus, Ximena
Barraza, Natalia
Calco, Valerie
Houy, Sébastien
Couve, Eduardo
Neely, Alan
Martínez, Agustín D.
Gasman, Stéphane
Cárdenas, Ana M.
Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title_full Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title_fullStr Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title_full_unstemmed Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title_short Dynamin-2 Regulates Fusion Pore Expansion and Quantal Release through a Mechanism that Involves Actin Dynamics in Neuroendocrine Chromaffin Cells
title_sort dynamin-2 regulates fusion pore expansion and quantal release through a mechanism that involves actin dynamics in neuroendocrine chromaffin cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3734226/
https://www.ncbi.nlm.nih.gov/pubmed/23940613
http://dx.doi.org/10.1371/journal.pone.0070638
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