The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER
Summary: Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from discrete subdomains. Lipid bilayer remodeling necessary for this process is driven initially by membrane pe...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2023-06-01
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| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723006460 |
| _version_ | 1827929036252250112 |
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| author | William Kasberg Peter Luong Michael G. Hanna Kayla Minushkin Annabelle Tsao Raakhee Shankar Samuel Block Anjon Audhya |
| author_facet | William Kasberg Peter Luong Michael G. Hanna Kayla Minushkin Annabelle Tsao Raakhee Shankar Samuel Block Anjon Audhya |
| author_sort | William Kasberg |
| collection | DOAJ |
| description | Summary: Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from discrete subdomains. Lipid bilayer remodeling necessary for this process is driven initially by membrane penetration mediated by the Sar1 GTPase and further stabilized by assembly of a multilayered complex of several COPII proteins. However, the relative contributions of these distinct factors to transport carrier formation and protein trafficking remain unclear. Here, we demonstrate that anterograde cargo transport from the ER continues in the absence of Sar1, although the efficiency of this process is dramatically reduced. Specifically, secretory cargoes are retained nearly five times longer at ER subdomains when Sar1 is depleted, but they ultimately remain capable of being translocated to the perinuclear region of cells. Taken together, our findings highlight alternative mechanisms by which COPII promotes transport carrier biogenesis. |
| first_indexed | 2024-03-13T06:17:10Z |
| format | Article |
| id | doaj.art-f52889c7fb184429a32bc105b971be31 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-03-13T06:17:10Z |
| publishDate | 2023-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-f52889c7fb184429a32bc105b971be312023-06-11T04:14:28ZengElsevierCell Reports2211-12472023-06-01426112635The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ERWilliam Kasberg0Peter Luong1Michael G. Hanna2Kayla Minushkin3Annabelle Tsao4Raakhee Shankar5Samuel Block6Anjon Audhya7Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USADepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706, USA; Corresponding authorSummary: Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from discrete subdomains. Lipid bilayer remodeling necessary for this process is driven initially by membrane penetration mediated by the Sar1 GTPase and further stabilized by assembly of a multilayered complex of several COPII proteins. However, the relative contributions of these distinct factors to transport carrier formation and protein trafficking remain unclear. Here, we demonstrate that anterograde cargo transport from the ER continues in the absence of Sar1, although the efficiency of this process is dramatically reduced. Specifically, secretory cargoes are retained nearly five times longer at ER subdomains when Sar1 is depleted, but they ultimately remain capable of being translocated to the perinuclear region of cells. Taken together, our findings highlight alternative mechanisms by which COPII promotes transport carrier biogenesis.http://www.sciencedirect.com/science/article/pii/S2211124723006460CP: Cell biology |
| spellingShingle | William Kasberg Peter Luong Michael G. Hanna Kayla Minushkin Annabelle Tsao Raakhee Shankar Samuel Block Anjon Audhya The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER Cell Reports CP: Cell biology |
| title | The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER |
| title_full | The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER |
| title_fullStr | The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER |
| title_full_unstemmed | The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER |
| title_short | The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER |
| title_sort | sar1 gtpase is dispensable for copii dependent cargo export from the er |
| topic | CP: Cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124723006460 |
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