Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/81274
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dc.contributorDepartment of Applied Biology and Chemical Technology-
dc.creatorNiu, LL-
dc.creatorMa, TJ-
dc.creatorYang, F-
dc.creatorYan, B-
dc.creatorTang, X-
dc.creatorYin, HD-
dc.creatorWu, Q-
dc.creatorHuang, Y-
dc.creatorYao, ZP-
dc.creatorWang, JF-
dc.creatorGuo, YS-
dc.creatorHu, JJ-
dc.date.accessioned2019-09-20T00:54:51Z-
dc.date.available2019-09-20T00:54:51Z-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10397/81274-
dc.language.isoenen_US
dc.publisherNational Academy of Sciencesen_US
dc.rightsCopyright © 2019 the Author(s). Published by PNAS.en_US
dc.rightsThis open access article is distributed under Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/).en_US
dc.rightsThe 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.1908409116en_US
dc.subjectEndoplasmic reticulumen_US
dc.subjectAtlastinen_US
dc.subjectMembrane tensionen_US
dc.subjectCOPII formationen_US
dc.subjectProtein mobilityen_US
dc.titleAtlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulumen_US
dc.typeConference Paperen_US
dc.identifier.spage14029-
dc.identifier.epage14038-
dc.identifier.volume116-
dc.identifier.issue28-
dc.identifier.doi10.1073/pnas.1908409116-
dcterms.abstractEndoplasmic 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.-
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationProceedings of the National Academy of Sciences of the United States of America, 9 July 2019, v. 116, no. 28, p. 14029-14038-
dcterms.isPartOfProceedings of the National Academy of Sciences of the United States of America-
dcterms.issued2019-
dc.identifier.isiWOS:000474535700055-
dc.identifier.scopus2-s2.0-85068621163-
dc.identifier.pmid31239341-
dc.identifier.eissn1091-6490-
dc.description.validate201909 bcrc-
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumberOA_Scopus/WOSen_US
dc.description.pubStatusPublisheden_US
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