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  A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly

Dodonova, S. O., Diestelkoetter-Bachert, P., von Appen, A., Hagen, W. J. H., Beck, R., Beck, M., et al. (2015). A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly. Science, 349(6244), 195-198. doi:10.1126/science.aab1121.

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Dodonova, S. O., Author
Diestelkoetter-Bachert, P., Author
von Appen, A., Author
Hagen, W. J. H., Author
Beck, R., Author
Beck, M., Author
Wieland, F., Author
Briggs, John A. G.1, Author           
Affiliations:
1European Molecular Biology Laboratory, External Organizations, ou_3346677              

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Free keywords: dilysine retrieval motifs clathrin adapter complex cryoelectron tomography molecular architecture conformational-change crystal-structure recruitment transport binding model Science & Technology - Other Topics
 Abstract: Transport of material within cells is mediated by trafficking vesicles that bud from one cellular compartment and fuse with another. Formation of a trafficking vesicle is driven by membrane coats that localize cargo and polymerize into cages to bend the membrane. Although extensive structural information is available for components of these coats, the heterogeneity of trafficking vesicles has prevented an understanding of how complete membrane coats assemble on the membrane. We combined cryo-electron tomography, subtomogram averaging, and cross-linking mass spectrometry to derive a complete model of the assembled coat protein complex I (COPI) coat involved in traffic between the Golgi and the endoplasmic reticulum. The highly interconnected COPI coat structure contradicted the current "adaptor-and-cage" understanding of coated vesicle formation.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000357664300046
DOI: 10.1126/science.aab1121
ISSN: 0036-8075
 Degree: -

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Title: Science
  Alternative Title : Science
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 349 (6244) Sequence Number: - Start / End Page: 195 - 198 Identifier: -