Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat
Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also cont...
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| Format: | Article |
| Language: | en_US |
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Rockefeller University Press
2014
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| Online Access: | http://hdl.handle.net/1721.1/85628 https://orcid.org/0000-0001-8012-1512 |
| _version_ | 1826193975527079936 |
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| author | Schwartz, Thomas Whittle, James Richardson Ross |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Schwartz, Thomas Whittle, James Richardson Ross |
| author_sort | Schwartz, Thomas |
| collection | MIT |
| description | Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-Å resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1–ACE1 interface is observed both in the prior structure of Sec13–Sec31 and in Sec13–Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-Å resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13–Sec31 coat. |
| first_indexed | 2024-09-23T09:48:37Z |
| format | Article |
| id | mit-1721.1/85628 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:48:37Z |
| publishDate | 2014 |
| publisher | Rockefeller University Press |
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| spelling | mit-1721.1/856282022-09-30T16:56:41Z Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat Schwartz, Thomas Whittle, James Richardson Ross Massachusetts Institute of Technology. Department of Biology Whittle, James R.R. Schwartz, Thomas Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-Å resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1–ACE1 interface is observed both in the prior structure of Sec13–Sec31 and in Sec13–Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-Å resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13–Sec31 coat. Pew Charitable Trusts (Pew Scholar Award) National Center for Research Resources (U.S.) (Award RR-15301) United States. Dept. of Energy. Office of Basic Energy Sciences (Contract DE-AC02-06CH11357) 2014-03-14T16:07:58Z 2014-03-14T16:07:58Z 2010-08 2010-03 Article http://purl.org/eprint/type/JournalArticle 0021-9525 1540-8140 http://hdl.handle.net/1721.1/85628 Whittle, J. R. R., and T. U. Schwartz. “Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat.” The Journal of Cell Biology 190, no. 3 (August 9, 2010): 347-361. https://orcid.org/0000-0001-8012-1512 en_US http://dx.doi.org/10.1083/jcb.201003092 The Journal of Cell Biology Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf Rockefeller University Press Rockefeller University Press |
| spellingShingle | Schwartz, Thomas Whittle, James Richardson Ross Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title | Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title_full | Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title_fullStr | Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title_full_unstemmed | Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title_short | Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat |
| title_sort | structure of the sec13 sec16 edge element a template for assembly of the copii vesicle coat |
| url | http://hdl.handle.net/1721.1/85628 https://orcid.org/0000-0001-8012-1512 |
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