Subtomogram averaging of COPII assemblies reveals how coat organization dictates membrane shape
Author:
Funder
Royal Society
Wellcome Trust
Medical Research Council
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/s41467-018-06577-4.pdf
Reference31 articles.
1. Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895–907 (1994).
2. Zanetti, G., Pahuja, K. B., Studer, S., Shim, S. & Schekman, R. COPII and the regulation of protein sorting in mammals. Nat. Cell Biol. 14, 20–28 (2012).
3. Lee, M. C. S. et al. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122, 605–617 (2005).
4. Zanetti, G. et al. The structure of the COPII transport-vesicle coat assembled on membranes. eLife 2, e00951 (2013).
5. Stagg, S. M. et al. Structure of the Sec13/31 COPII coat cage. Nature 439, 234–238 (2006).
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