Mechanical strain stimulates COPII‐dependent secretory trafficking via Rac1
Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical s...
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| Published in | The EMBO journal Vol. 41; no. 18; pp. e110596 - n/a |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
15.09.2022
Springer Nature B.V John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0261-4189 1460-2075 1460-2075 |
| DOI | 10.15252/embj.2022110596 |
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| Abstract | Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER‐to‐Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER‐localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER‐to‐Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER.
Synopsis
Whether and how mechanical signals regulate the endoplasmic reticulum (ER) is incompletely understood. Here, mechanical stress is found to increase ER exit site (ERES) numbers and secretory trafficking to respond with surface expansion.
Mechanotransduction to ERES involves the small GTPase Rac1.
Rac1 localizes to the ER where it forms a complex with Sar1.
Rac1 stimulates the formation of COPII carriers.
Blocking ERES renders cells more sensitive to mechanical strain.
Graphical Abstract
Mechanical strain regulates the number of endoplasmic reticulum exit sites through small GTPase heterodimerization. |
|---|---|
| AbstractList | Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER-to-Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER-localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER-to-Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER‐to‐Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER‐localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER‐to‐Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. image Whether and how mechanical signals regulate the endoplasmic reticulum (ER) is incompletely understood. Here, mechanical stress is found to increase ER exit site (ERES) numbers and secretory trafficking to respond with surface expansion. Mechanotransduction to ERES involves the small GTPase Rac1. Rac1 localizes to the ER where it forms a complex with Sar1. Rac1 stimulates the formation of COPII carriers. Blocking ERES renders cells more sensitive to mechanical strain. Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER‐to‐Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER‐localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER‐to‐Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. Mechanical strain regulates the number of endoplasmic reticulum exit sites through small GTPase heterodimerization. Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER-to-Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER-localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER-to-Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER.Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER-to-Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER-localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER-to-Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER‐to‐Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER‐localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER‐to‐Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. Synopsis Whether and how mechanical signals regulate the endoplasmic reticulum (ER) is incompletely understood. Here, mechanical stress is found to increase ER exit site (ERES) numbers and secretory trafficking to respond with surface expansion. Mechanotransduction to ERES involves the small GTPase Rac1. Rac1 localizes to the ER where it forms a complex with Sar1. Rac1 stimulates the formation of COPII carriers. Blocking ERES renders cells more sensitive to mechanical strain. Graphical Abstract Mechanical strain regulates the number of endoplasmic reticulum exit sites through small GTPase heterodimerization. Cells are constantly exposed to various chemical and physical stimuli. While much has been learned about the biochemical factors that regulate secretory trafficking from the endoplasmic reticulum (ER), much less is known about whether and how this trafficking is subject to regulation by mechanical signals. Here, we show that subjecting cells to mechanical strain both induces the formation of ER exit sites (ERES) and accelerates ER‐to‐Golgi trafficking. We found that cells with impaired ERES function were less capable of expanding their surface area when placed under mechanical stress and were more prone to develop plasma membrane defects when subjected to stretching. Thus, coupling of ERES function to mechanotransduction appears to confer resistance of cells to mechanical stress. Furthermore, we show that the coupling of mechanotransduction to ERES formation was mediated via a previously unappreciated ER‐localized pool of the small GTPase Rac1. Mechanistically, we show that Rac1 interacts with the small GTPase Sar1 to drive budding of COPII carriers and stimulates ER‐to‐Golgi transport. This interaction therefore represents an unprecedented link between mechanical strain and export from the ER. Synopsis Whether and how mechanical signals regulate the endoplasmic reticulum (ER) is incompletely understood. Here, mechanical stress is found to increase ER exit site (ERES) numbers and secretory trafficking to respond with surface expansion. Mechanotransduction to ERES involves the small GTPase Rac1. Rac1 localizes to the ER where it forms a complex with Sar1. Rac1 stimulates the formation of COPII carriers. Blocking ERES renders cells more sensitive to mechanical strain. Mechanical strain regulates the number of endoplasmic reticulum exit sites through small GTPase heterodimerization. |
| Author | Kahlhofer, Jennifer C Fankhauser, Daniela Eriksson, Leif Djaerff, Elena Geley, Stephan Mahdizadeh, Sayyed Jalil Reiterer, Veronika Kazanietz, Marcelo G Felder, Edward Roca‐Cusachs, Pere Teis, David Farhan, Hesso Phuyal, Santosh Parizadeh, Amirabbas Le Roux, Anabel‐Lise Baker, Martin J |
| AuthorAffiliation | 2 Institute for Bioengineering of Catalonia (IBEC) the Barcelona Institute of Technology (BIST) Barcelona Spain 5 Department of chemistry and molecular biology University of Gothenburg Gothenburg Sweden 8 Universitat de Barcelona Barcelona Spain 6 Institute of General Physiology University of Ulm Ulm Germany 3 Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine University of Pennsylvania Philadelphia Pennsylvania USA 1 Institute of Basic Medical Sciences University of Oslo Oslo Norway 4 Institute of Pathophysiology Medical University of Innsbruck Innsbruck Austria 7 Institute of Cell Biology Medical University of Innsbruck Innsbruck Austria |
| AuthorAffiliation_xml | – name: 6 Institute of General Physiology University of Ulm Ulm Germany – name: 4 Institute of Pathophysiology Medical University of Innsbruck Innsbruck Austria – name: 8 Universitat de Barcelona Barcelona Spain – name: 1 Institute of Basic Medical Sciences University of Oslo Oslo Norway – name: 7 Institute of Cell Biology Medical University of Innsbruck Innsbruck Austria – name: 5 Department of chemistry and molecular biology University of Gothenburg Gothenburg Sweden – name: 2 Institute for Bioengineering of Catalonia (IBEC) the Barcelona Institute of Technology (BIST) Barcelona Spain – name: 3 Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine University of Pennsylvania Philadelphia Pennsylvania USA |
| Author_xml | – sequence: 1 givenname: Santosh orcidid: 0000-0002-1922-2098 surname: Phuyal fullname: Phuyal, Santosh email: santosh.phuyal@medisin.uio.no organization: Institute of Basic Medical Sciences, University of Oslo – sequence: 2 givenname: Elena surname: Djaerff fullname: Djaerff, Elena organization: Institute of Basic Medical Sciences, University of Oslo – sequence: 3 givenname: Anabel‐Lise orcidid: 0000-0003-4152-5658 surname: Le Roux fullname: Le Roux, Anabel‐Lise organization: Institute for Bioengineering of Catalonia (IBEC), the Barcelona Institute of Technology (BIST) – sequence: 4 givenname: Martin J orcidid: 0000-0002-9743-6294 surname: Baker fullname: Baker, Martin J organization: Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine, University of Pennsylvania – sequence: 5 givenname: Daniela surname: Fankhauser fullname: Fankhauser, Daniela organization: Institute of Pathophysiology, Medical University of Innsbruck – sequence: 6 givenname: Sayyed Jalil orcidid: 0000-0002-4844-6234 surname: Mahdizadeh fullname: Mahdizadeh, Sayyed Jalil organization: Department of chemistry and molecular biology, University of Gothenburg – sequence: 7 givenname: Veronika surname: Reiterer fullname: Reiterer, Veronika organization: Institute of Pathophysiology, Medical University of Innsbruck – sequence: 8 givenname: Amirabbas surname: Parizadeh fullname: Parizadeh, Amirabbas organization: Institute of Pathophysiology, Medical University of Innsbruck – sequence: 9 givenname: Edward orcidid: 0000-0002-1831-2008 surname: Felder fullname: Felder, Edward organization: Institute of General Physiology, University of Ulm – sequence: 10 givenname: Jennifer C surname: Kahlhofer fullname: Kahlhofer, Jennifer C organization: Institute of Cell Biology, Medical University of Innsbruck – sequence: 11 givenname: David orcidid: 0000-0002-8181-0253 surname: Teis fullname: Teis, David organization: Institute of Cell Biology, Medical University of Innsbruck – sequence: 12 givenname: Marcelo G orcidid: 0000-0001-8779-017X surname: Kazanietz fullname: Kazanietz, Marcelo G organization: Department of Systems Pharmacology and Translational Therapeutics, Perelman School of Medicine, University of Pennsylvania – sequence: 13 givenname: Stephan surname: Geley fullname: Geley, Stephan organization: Institute of Pathophysiology, Medical University of Innsbruck – sequence: 14 givenname: Leif orcidid: 0000-0001-5654-3109 surname: Eriksson fullname: Eriksson, Leif organization: Department of chemistry and molecular biology, University of Gothenburg – sequence: 15 givenname: Pere orcidid: 0000-0001-6947-961X surname: Roca‐Cusachs fullname: Roca‐Cusachs, Pere email: proca@ibecbarcelona.eu organization: Institute for Bioengineering of Catalonia (IBEC), the Barcelona Institute of Technology (BIST), Universitat de Barcelona – sequence: 16 givenname: Hesso orcidid: 0000-0002-0889-8463 surname: Farhan fullname: Farhan, Hesso email: hesso.farhan@i-med.ac.at organization: Institute of Basic Medical Sciences, University of Oslo, Institute of Pathophysiology, Medical University of Innsbruck |
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| IngestDate | Thu Aug 21 06:55:50 EDT 2025 Thu Aug 21 18:39:58 EDT 2025 Thu Aug 29 03:27:19 EDT 2024 Fri Jul 11 03:54:38 EDT 2025 Fri Jul 25 10:56:26 EDT 2025 Mon Jul 21 06:03:55 EDT 2025 Tue Jul 01 01:47:23 EDT 2025 Thu Apr 24 23:00:30 EDT 2025 Wed Jan 22 16:23:56 EST 2025 Fri Feb 21 02:37:31 EST 2025 |
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| Issue | 18 |
| Keywords | mechanobiology COPII endoplasmic reticulum |
| Language | English |
| License | Attribution 2022 The Authors. Published under the terms of the CC BY 4.0 license. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
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| PublicationTitle | The EMBO journal |
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| Publisher | Nature Publishing Group UK Springer Nature B.V John Wiley and Sons Inc |
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| SubjectTerms | Biochemistry & Molecular Biology Biologi Biological Sciences Biological Transport Cell Biology cells COP-Coated Vesicles - metabolism COPII Coupling docking EMBO20 Endoplasmic reticulum Endoplasmic Reticulum - metabolism fast interaction refinement Golgi apparatus Golgi Apparatus - metabolism gtpase Guanosine triphosphatases Mechanical stimuli mechanobiology Mechanotransduction Mechanotransduction, Cellular Membrane & Trafficking Monomeric GTP-Binding Proteins - metabolism proliferation protein Protein Transport - physiology Rac1 protein reticulum exit sites Strain Trafficking web server |
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| Title | Mechanical strain stimulates COPII‐dependent secretory trafficking via Rac1 |
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