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Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex
The Golgi complex comprises a connected ribbon of stacked cisternal membranes localized to the perinuclear region in most vertebrate cells. The position and morphology of this organelle depends upon interactions with microtubules and the actin cytoskeleton. In contrast, we know relatively little abo...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10617613/ https://www.ncbi.nlm.nih.gov/pubmed/37732478 http://dx.doi.org/10.1242/jcs.260577 |
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author | Vitali, Teresa Sanchez-Alvarez, Rosa Witkos, Tomasz M. Bantounas, Ioannis Cutiongco, Marie F. A. Dudek, Michal Yan, Guanhua Mironov, Alexander A. Swift, Joe Lowe, Martin |
author_facet | Vitali, Teresa Sanchez-Alvarez, Rosa Witkos, Tomasz M. Bantounas, Ioannis Cutiongco, Marie F. A. Dudek, Michal Yan, Guanhua Mironov, Alexander A. Swift, Joe Lowe, Martin |
author_sort | Vitali, Teresa |
collection | PubMed |
description | The Golgi complex comprises a connected ribbon of stacked cisternal membranes localized to the perinuclear region in most vertebrate cells. The position and morphology of this organelle depends upon interactions with microtubules and the actin cytoskeleton. In contrast, we know relatively little about the relationship of the Golgi complex with intermediate filaments (IFs). In this study, we show that the Golgi is in close physical proximity to vimentin IFs in cultured mouse and human cells. We also show that the trans-Golgi network coiled-coil protein GORAB can physically associate with vimentin IFs. Loss of vimentin and/or GORAB had a modest effect upon Golgi structure at the steady state. The Golgi underwent more rapid disassembly upon chemical disruption with brefeldin A or nocodazole, and slower reassembly upon drug washout, in vimentin knockout cells. Moreover, loss of vimentin caused reduced Golgi ribbon integrity when cells were cultured on high-stiffness hydrogels, which was exacerbated by loss of GORAB. These results indicate that vimentin IFs contribute to the structural stability of the Golgi complex and suggest a role for GORAB in this process. |
format | Online Article Text |
id | pubmed-10617613 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-106176132023-11-01 Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex Vitali, Teresa Sanchez-Alvarez, Rosa Witkos, Tomasz M. Bantounas, Ioannis Cutiongco, Marie F. A. Dudek, Michal Yan, Guanhua Mironov, Alexander A. Swift, Joe Lowe, Martin J Cell Sci Research Article The Golgi complex comprises a connected ribbon of stacked cisternal membranes localized to the perinuclear region in most vertebrate cells. The position and morphology of this organelle depends upon interactions with microtubules and the actin cytoskeleton. In contrast, we know relatively little about the relationship of the Golgi complex with intermediate filaments (IFs). In this study, we show that the Golgi is in close physical proximity to vimentin IFs in cultured mouse and human cells. We also show that the trans-Golgi network coiled-coil protein GORAB can physically associate with vimentin IFs. Loss of vimentin and/or GORAB had a modest effect upon Golgi structure at the steady state. The Golgi underwent more rapid disassembly upon chemical disruption with brefeldin A or nocodazole, and slower reassembly upon drug washout, in vimentin knockout cells. Moreover, loss of vimentin caused reduced Golgi ribbon integrity when cells were cultured on high-stiffness hydrogels, which was exacerbated by loss of GORAB. These results indicate that vimentin IFs contribute to the structural stability of the Golgi complex and suggest a role for GORAB in this process. The Company of Biologists Ltd 2023-10-18 /pmc/articles/PMC10617613/ /pubmed/37732478 http://dx.doi.org/10.1242/jcs.260577 Text en © 2023. Published by The Company of Biologists Ltd https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0 (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Vitali, Teresa Sanchez-Alvarez, Rosa Witkos, Tomasz M. Bantounas, Ioannis Cutiongco, Marie F. A. Dudek, Michal Yan, Guanhua Mironov, Alexander A. Swift, Joe Lowe, Martin Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title | Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title_full | Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title_fullStr | Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title_full_unstemmed | Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title_short | Vimentin intermediate filaments provide structural stability to the mammalian Golgi complex |
title_sort | vimentin intermediate filaments provide structural stability to the mammalian golgi complex |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10617613/ https://www.ncbi.nlm.nih.gov/pubmed/37732478 http://dx.doi.org/10.1242/jcs.260577 |
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