The Role of Munc18-1 and Its Orthologs in Modulation of Cortical F-Actin in Chromaffin Cells

J. Kurps, H. de Wit

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Munc18-1 was originally described as an essential docking factor in chromaffin cells. Recent findings showed that Munc18-1 has an additional role in the regulation of the cortical F-actin network, which is thought to function as a physical barrier preventing secretory vesicles from access to their release sites under resting conditions. In our review, we discuss whether this function is evolutionarily conserved in all Sec1/ Munc18-like (SM) proteins. In addition, we introduce a new quantification method that improves the analysis of cortical filamentous actin (F-actin) in comparison with existing methods. Since the docking process is highly evolutionarily conserved in the SM protein superfamily, we use our novel quantification method to investigate whether the F-actin-regulating function is similarly conserved among SM proteins. Our preliminary data suggest that the regulation of cortical F-actin is a shared function of SM proteins, and we propose a way to gain more insight in the molecular mechanism underlying the Munc18-1-mediated cortical F-actin regulation. © Springer Science+Business Media, LLC 2012.
Original languageEnglish
Pages (from-to)339-346
JournalJournal of Molecular Neuroscience
Volume48
Issue number2
DOIs
Publication statusPublished - 2012

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Munc18 Proteins
Chromaffin Cells
Actins
Architectural Accessibility
Secretory Vesicles

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title = "The Role of Munc18-1 and Its Orthologs in Modulation of Cortical F-Actin in Chromaffin Cells",
abstract = "Munc18-1 was originally described as an essential docking factor in chromaffin cells. Recent findings showed that Munc18-1 has an additional role in the regulation of the cortical F-actin network, which is thought to function as a physical barrier preventing secretory vesicles from access to their release sites under resting conditions. In our review, we discuss whether this function is evolutionarily conserved in all Sec1/ Munc18-like (SM) proteins. In addition, we introduce a new quantification method that improves the analysis of cortical filamentous actin (F-actin) in comparison with existing methods. Since the docking process is highly evolutionarily conserved in the SM protein superfamily, we use our novel quantification method to investigate whether the F-actin-regulating function is similarly conserved among SM proteins. Our preliminary data suggest that the regulation of cortical F-actin is a shared function of SM proteins, and we propose a way to gain more insight in the molecular mechanism underlying the Munc18-1-mediated cortical F-actin regulation. {\circledC} Springer Science+Business Media, LLC 2012.",
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The Role of Munc18-1 and Its Orthologs in Modulation of Cortical F-Actin in Chromaffin Cells. / Kurps, J.; de Wit, H.

In: Journal of Molecular Neuroscience, Vol. 48, No. 2, 2012, p. 339-346.

Research output: Contribution to JournalArticleAcademicpeer-review

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AB - Munc18-1 was originally described as an essential docking factor in chromaffin cells. Recent findings showed that Munc18-1 has an additional role in the regulation of the cortical F-actin network, which is thought to function as a physical barrier preventing secretory vesicles from access to their release sites under resting conditions. In our review, we discuss whether this function is evolutionarily conserved in all Sec1/ Munc18-like (SM) proteins. In addition, we introduce a new quantification method that improves the analysis of cortical filamentous actin (F-actin) in comparison with existing methods. Since the docking process is highly evolutionarily conserved in the SM protein superfamily, we use our novel quantification method to investigate whether the F-actin-regulating function is similarly conserved among SM proteins. Our preliminary data suggest that the regulation of cortical F-actin is a shared function of SM proteins, and we propose a way to gain more insight in the molecular mechanism underlying the Munc18-1-mediated cortical F-actin regulation. © Springer Science+Business Media, LLC 2012.

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