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Title: Atlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulum
Authors: Niu, LL
Ma, TJ
Yang, F
Yan, B
Tang, X
Yin, HD 
Wu, Q 
Huang, Y
Yao, ZP 
Wang, JF
Guo, YS
Hu, JJ
Issue Date: 2019
Source: Proceedings of the National Academy of Sciences of the United States of America, 9 July 2019, v. 116, no. 28, p. 14029-14038
Abstract: 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.
Keywords: Endoplasmic reticulum
Atlastin
Membrane tension
COPII formation
Protein mobility
Publisher: National Academy of Sciences
Journal: Proceedings of the National Academy of Sciences of the United States of America 
ISSN: 0027-8424
EISSN: 1091-6490
DOI: 10.1073/pnas.1908409116
Rights: Copyright © 2019 the Author(s). Published by PNAS.
This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/).
The following publication Niu, L. L., Ma, T. J., Yang, F., Yan, B., Tang, X., Yin, H. D., . . . Hu, J. J. (2019). Atlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America, 116(28), 14029-14038 is available at https://dx.doi.org/10.1073/pnas.1908409116
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