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Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network

View ORCID ProfileJoshua Hutchings, Viktoriya G. Stancheva, Nick R. Brown, View ORCID ProfileAlan C.M. Cheung, View ORCID ProfileElizabeth A. Miller, View ORCID ProfileGiulia Zanetti
doi: https://doi.org/10.1101/2020.06.18.159608
Joshua Hutchings
1Institute of Structural and Molecular Biology, Birkbeck College, London
5Division of Biological Sciences, University of California San Diego, La Jolla, CA
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  • ORCID record for Joshua Hutchings
Viktoriya G. Stancheva
2MRC Laboratory of Molecular Biology, Cambridge
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Nick R. Brown
1Institute of Structural and Molecular Biology, Birkbeck College, London
3The Francis Crick Institute, London
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Alan C.M. Cheung
1Institute of Structural and Molecular Biology, Birkbeck College, London
4School of Biochemistry at the University of Bristol
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Elizabeth A. Miller
2MRC Laboratory of Molecular Biology, Cambridge
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Giulia Zanetti
1Institute of Structural and Molecular Biology, Birkbeck College, London
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  • ORCID record for Giulia Zanetti
  • For correspondence: g.zanetti@bbk.ac.uk
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Abstract

The COPII coat mediates Endoplasmic Reticulum (ER) to Golgi trafficking for thousands of proteins. Five essential coat proteins assemble at the ER into a characteristic two-layer architecture, which recruits cargo proteins whilst sculpting membrane carriers with diverse morphologies. How coat architecture drives membrane curvature whilst ensuring morphological plasticity is largely unknown, yet is central to understanding mechanisms of carrier formation. Here, we use an established reconstitution system to visualise the complete, membrane-assembled COPII coat with unprecedented detail by cryo-electron tomography and subtomogram averaging. We discover a network of interactions within and between coat layers, including multiple interfaces that were previously unknown. We reveal the physiological importance of these interactions using genetic and biochemical approaches. A newly resolved Sec31 C-terminal domain provides order to the coat and is essential to drive membrane curvature in cells. Moreover, a novel outer coat assembly mode provides a basis for coat adaptability to varying membrane curvatures. Furthermore, a newly resolved region of Sec23, which we term the L-loop, imparts coat stability and in part dictates membrane shape. Our results suggest these interactions collectively contribute to coat organisation and membrane curvature, providing a structural framework to understand regulatory mechanisms of COPII trafficking and secretion.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • The manuscript was revised according to reviewers comments

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted October 08, 2020.
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Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network
Joshua Hutchings, Viktoriya G. Stancheva, Nick R. Brown, Alan C.M. Cheung, Elizabeth A. Miller, Giulia Zanetti
bioRxiv 2020.06.18.159608; doi: https://doi.org/10.1101/2020.06.18.159608
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Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network
Joshua Hutchings, Viktoriya G. Stancheva, Nick R. Brown, Alan C.M. Cheung, Elizabeth A. Miller, Giulia Zanetti
bioRxiv 2020.06.18.159608; doi: https://doi.org/10.1101/2020.06.18.159608

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