Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 116, Issue 28, Pages 14029-14038Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1908409116
Keywords
endoplasmic reticulum; atlastin; membrane tension; COPII formation; protein mobility
Categories
Funding
- National Natural Science Foundation of China [31630020, 91854202, 31700729]
- National Key Research and Development Program [2016YFA0500201]
- Strategic Priority Research Program (pilot study) Biological basis of aging and therapeutic strategies of the Chinese Academy of Sciences [XDPB10]
- Research Grants Council (RGC) Hong Kong [26100315, 16101116, 16102218, AoE/M-05/12, C4002-17G]
- RGC Collaborative Research Fund [C5031-14E]
- University Research Facility in Chemical and Environmental Analysis of the Hong Kong Polytechnic University
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Endoplasmic reticulum (ER) membrane junctions are formed by the dynamin-like GTPase atlastin (ATL). Deletion of ATL results in long unbranched ER tubules in cells, and mutation of human ATL1 is linked to hereditary spastic paraplegia. Here, we demonstrate that COPII formation is drastically decreased in the periphery of ATL-deleted cells. ER export of cargo proteins becomes defective; ER exit site initiation is not affected, but many of the sites fail to recruit COPII subunits. The efficiency of cargo packaging into COPII vesicles is significantly reduced in cells lacking ATLs, or when the ER is transiently fragmented. Cargo is less mobile in the ER in the absence of ATL, but the cargo mobility and COPII formation can be restored by ATL R77A, which is capable of tethering, but not fusing, ER tubules. These findings suggest that the generation of ER junctions by ATL plays a critical role in maintaining the necessary mobility of ER contents to allow efficient packaging of cargo proteins into COPII vesicles.
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