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Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions
The actin and microtubule cytoskeletons play important roles in Golgi structure and function, but how they are connected remain poorly known. In this study, we investigated whether RAB6 GTPase, a Golgi-associated RAB involved in the regulation of several transport steps at the Golgi level, and two o...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5665954/ https://www.ncbi.nlm.nih.gov/pubmed/29093437 http://dx.doi.org/10.1038/s41467-017-01266-0 |
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author | Miserey-Lenkei, Stéphanie Bousquet, Hugo Pylypenko, Olena Bardin, Sabine Dimitrov, Ariane Bressanelli, Gaëlle Bonifay, Raja Fraisier, Vincent Guillou, Catherine Bougeret, Cécile Houdusse, Anne Echard, Arnaud Goud, Bruno |
author_facet | Miserey-Lenkei, Stéphanie Bousquet, Hugo Pylypenko, Olena Bardin, Sabine Dimitrov, Ariane Bressanelli, Gaëlle Bonifay, Raja Fraisier, Vincent Guillou, Catherine Bougeret, Cécile Houdusse, Anne Echard, Arnaud Goud, Bruno |
author_sort | Miserey-Lenkei, Stéphanie |
collection | PubMed |
description | The actin and microtubule cytoskeletons play important roles in Golgi structure and function, but how they are connected remain poorly known. In this study, we investigated whether RAB6 GTPase, a Golgi-associated RAB involved in the regulation of several transport steps at the Golgi level, and two of its effectors, Myosin IIA and KIF20A participate in the coupling between actin and microtubule cytoskeleton. We have previously shown that RAB6–Myosin IIA interaction is critical for the fission of RAB6-positive transport carriers from Golgi/TGN membranes. Here we show that KIF20A is also involved in the fission process and serves to anchor RAB6 on Golgi/TGN membranes near microtubule nucleating sites. We provide evidence that the fission events occur at a limited number of hotspots sites. Our results suggest that coupling between actin and microtubule cytoskeletons driven by Myosin II and KIF20A ensures the spatial coordination between RAB6-positive vesicles fission from Golgi/TGN membranes and their exit along microtubules. |
format | Online Article Text |
id | pubmed-5665954 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56659542017-11-07 Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions Miserey-Lenkei, Stéphanie Bousquet, Hugo Pylypenko, Olena Bardin, Sabine Dimitrov, Ariane Bressanelli, Gaëlle Bonifay, Raja Fraisier, Vincent Guillou, Catherine Bougeret, Cécile Houdusse, Anne Echard, Arnaud Goud, Bruno Nat Commun Article The actin and microtubule cytoskeletons play important roles in Golgi structure and function, but how they are connected remain poorly known. In this study, we investigated whether RAB6 GTPase, a Golgi-associated RAB involved in the regulation of several transport steps at the Golgi level, and two of its effectors, Myosin IIA and KIF20A participate in the coupling between actin and microtubule cytoskeleton. We have previously shown that RAB6–Myosin IIA interaction is critical for the fission of RAB6-positive transport carriers from Golgi/TGN membranes. Here we show that KIF20A is also involved in the fission process and serves to anchor RAB6 on Golgi/TGN membranes near microtubule nucleating sites. We provide evidence that the fission events occur at a limited number of hotspots sites. Our results suggest that coupling between actin and microtubule cytoskeletons driven by Myosin II and KIF20A ensures the spatial coordination between RAB6-positive vesicles fission from Golgi/TGN membranes and their exit along microtubules. Nature Publishing Group UK 2017-11-01 /pmc/articles/PMC5665954/ /pubmed/29093437 http://dx.doi.org/10.1038/s41467-017-01266-0 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Miserey-Lenkei, Stéphanie Bousquet, Hugo Pylypenko, Olena Bardin, Sabine Dimitrov, Ariane Bressanelli, Gaëlle Bonifay, Raja Fraisier, Vincent Guillou, Catherine Bougeret, Cécile Houdusse, Anne Echard, Arnaud Goud, Bruno Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title | Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title_full | Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title_fullStr | Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title_full_unstemmed | Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title_short | Coupling fission and exit of RAB6 vesicles at Golgi hotspots through kinesin-myosin interactions |
title_sort | coupling fission and exit of rab6 vesicles at golgi hotspots through kinesin-myosin interactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5665954/ https://www.ncbi.nlm.nih.gov/pubmed/29093437 http://dx.doi.org/10.1038/s41467-017-01266-0 |
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