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9 angstrom structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.

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Dodonova,  S. O.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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2463642.pdf
(Publisher version), 7MB

Supplementary Material (public)

2463642_Suppl.pdf
(Supplementary material), 16MB

Citation

Dodonova, S. O., Aderhold, P., Kopp, J., Ganeva, I., Röhling, S., Hagen, W. J. H., et al. (2017). 9 angstrom structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. eLife, 6: e26691. doi:10.7554/eLife.26691.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-9BE1-D
Abstract
COPI coated vesicles mediate trafficking within the Golgi apparatus and between the Golgi and the endoplasmic reticulum. Assembly of a COPI coated vesicle is initiated by the small GTPase Arf1 that recruits the coatomer complex to the membrane, triggering polymerization and budding. The vesicle uncoats before fusion with a target membrane. Coat components are structurally conserved between COPI and clathrin/adaptor proteins. Using cryo-electron tomography and subtomogram averaging, we determined the structure of the COPI coat assembled on membranes in vitro at 9 angstrom resolution. We also obtained a 2.57 angstrom resolution crystal structure of beta delta-COP. By combining these structures we built a molecular model of the coat. We additionally determined the coat structure in the presence of ArfGAP proteins that regulate coat dissociation. We found that Arf1 occupies contrasting molecular environments within the coat, leading us to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.