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Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana
The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3571873/ https://www.ncbi.nlm.nih.gov/pubmed/23283982 http://dx.doi.org/10.1091/mbc.E12-06-0492 |
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author | Fendrych, Matyáš Synek, Lukáš Pečenková, Tamara Drdová, Edita Janková Sekereš, Juraj de Rycke, Riet Nowack, Moritz K. Žárský, Viktor |
author_facet | Fendrych, Matyáš Synek, Lukáš Pečenková, Tamara Drdová, Edita Janková Sekereš, Juraj de Rycke, Riet Nowack, Moritz K. Žárský, Viktor |
author_sort | Fendrych, Matyáš |
collection | PubMed |
description | The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocyst foci were independent of cytoskeleton, although prolonged actin disruption led to changes in exocyst localization. Exocyst foci partially overlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites without vesicles, as indicated by electron microscopy and drug treatments, supporting the concept of the exocyst functioning as a dynamic particle. We observed a decrease of SEC6–green fluorescent protein foci in an exo70A1 exocyst mutant. Finally, we documented decreased VAMP721 trafficking to the plasma membrane in exo70A1 and exo84b mutants. Our data support the concept that the exocyst-complex subunits dynamically dock and undock at the plasma membrane to create sites primed for vesicle tethering. |
format | Online Article Text |
id | pubmed-3571873 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-35718732013-04-30 Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana Fendrych, Matyáš Synek, Lukáš Pečenková, Tamara Drdová, Edita Janková Sekereš, Juraj de Rycke, Riet Nowack, Moritz K. Žárský, Viktor Mol Biol Cell Articles The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocyst foci were independent of cytoskeleton, although prolonged actin disruption led to changes in exocyst localization. Exocyst foci partially overlapped with vesicles visualized by VAMP721 v-SNARE, but the majority of the foci represent sites without vesicles, as indicated by electron microscopy and drug treatments, supporting the concept of the exocyst functioning as a dynamic particle. We observed a decrease of SEC6–green fluorescent protein foci in an exo70A1 exocyst mutant. Finally, we documented decreased VAMP721 trafficking to the plasma membrane in exo70A1 and exo84b mutants. Our data support the concept that the exocyst-complex subunits dynamically dock and undock at the plasma membrane to create sites primed for vesicle tethering. The American Society for Cell Biology 2013-02-15 /pmc/articles/PMC3571873/ /pubmed/23283982 http://dx.doi.org/10.1091/mbc.E12-06-0492 Text en © 2013 Fendrych et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Fendrych, Matyáš Synek, Lukáš Pečenková, Tamara Drdová, Edita Janková Sekereš, Juraj de Rycke, Riet Nowack, Moritz K. Žárský, Viktor Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title | Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title_full | Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title_fullStr | Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title_full_unstemmed | Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title_short | Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana |
title_sort | visualization of the exocyst complex dynamics at the plasma membrane of arabidopsis thaliana |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3571873/ https://www.ncbi.nlm.nih.gov/pubmed/23283982 http://dx.doi.org/10.1091/mbc.E12-06-0492 |
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