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A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi
Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi. Besides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the formation of long (∼3 µ...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469610/ https://www.ncbi.nlm.nih.gov/pubmed/28428254 http://dx.doi.org/10.1091/mbc.E16-12-0863 |
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author | Bottanelli, Francesca Kilian, Nicole Ernst, Andreas M. Rivera-Molina, Felix Schroeder, Lena K. Kromann, Emil B. Lessard, Mark D. Erdmann, Roman S. Schepartz, Alanna Baddeley, David Bewersdorf, Joerg Toomre, Derek Rothman, James E. |
author_facet | Bottanelli, Francesca Kilian, Nicole Ernst, Andreas M. Rivera-Molina, Felix Schroeder, Lena K. Kromann, Emil B. Lessard, Mark D. Erdmann, Roman S. Schepartz, Alanna Baddeley, David Bewersdorf, Joerg Toomre, Derek Rothman, James E. |
author_sort | Bottanelli, Francesca |
collection | PubMed |
description | Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi. Besides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the formation of long (∼3 µm), thin (∼110 nm diameter) tubular carriers. The anterograde and retrograde tubular carriers are both largely free of the classical Golgi coat proteins coatomer (COPI) and clathrin. Instead, they contain ARF1 along their entire length at a density estimated to be in the range of close packing. Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form. Dynamic confocal and stimulated emission depletion imaging shows that ARF1-rich tubular compartments fall into two distinct classes containing 1) anterograde cargoes and clathrin clusters or 2) retrograde cargoes and coatomer clusters. |
format | Online Article Text |
id | pubmed-5469610 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-54696102017-08-30 A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi Bottanelli, Francesca Kilian, Nicole Ernst, Andreas M. Rivera-Molina, Felix Schroeder, Lena K. Kromann, Emil B. Lessard, Mark D. Erdmann, Roman S. Schepartz, Alanna Baddeley, David Bewersdorf, Joerg Toomre, Derek Rothman, James E. Mol Biol Cell Articles Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi. Besides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the formation of long (∼3 µm), thin (∼110 nm diameter) tubular carriers. The anterograde and retrograde tubular carriers are both largely free of the classical Golgi coat proteins coatomer (COPI) and clathrin. Instead, they contain ARF1 along their entire length at a density estimated to be in the range of close packing. Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form. Dynamic confocal and stimulated emission depletion imaging shows that ARF1-rich tubular compartments fall into two distinct classes containing 1) anterograde cargoes and clathrin clusters or 2) retrograde cargoes and coatomer clusters. The American Society for Cell Biology 2017-06-15 /pmc/articles/PMC5469610/ /pubmed/28428254 http://dx.doi.org/10.1091/mbc.E16-12-0863 Text en © 2017 Bottanelli 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 for Cell Biology. |
spellingShingle | Articles Bottanelli, Francesca Kilian, Nicole Ernst, Andreas M. Rivera-Molina, Felix Schroeder, Lena K. Kromann, Emil B. Lessard, Mark D. Erdmann, Roman S. Schepartz, Alanna Baddeley, David Bewersdorf, Joerg Toomre, Derek Rothman, James E. A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title | A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title_full | A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title_fullStr | A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title_full_unstemmed | A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title_short | A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi |
title_sort | novel physiological role for arf1 in the formation of bidirectional tubules from the golgi |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469610/ https://www.ncbi.nlm.nih.gov/pubmed/28428254 http://dx.doi.org/10.1091/mbc.E16-12-0863 |
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