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  The Structures of COPI-Coated Vesicles Reveal Alternate Coatomer Conformations and Interactions

Faini, M., Prinz, S., Beck, R., Schorb, M., Riches, J. D., Bacia, K., et al. (2012). The Structures of COPI-Coated Vesicles Reveal Alternate Coatomer Conformations and Interactions. Science, 336(6087), 1451-1454. doi:10.1126/science.1221443.

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 Creators:
Faini, M., Author
Prinz, S., Author
Beck, R., Author
Schorb, M., Author
Riches, J. D., Author
Bacia, K., Author
Brugger, B., Author
Wieland, F. T., Author
Briggs, John A. G.1, Author           
Affiliations:
1European Molecular Biology Laboratory, External Organizations, ou_3346677              

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Free keywords: cryoelectron tomography clathrin transport complexes mechanism cage Science & Technology - Other Topics
 Abstract: Transport between compartments of eukaryotic cells is mediated by coated vesicles. The archetypal protein coats COPI, COPII, and clathrin are conserved from yeast to human. Structural studies of COPII and clathrin coats assembled in vitro without membranes suggest that coat components assemble regular cages with the same set of interactions between components. Detailed three-dimensional structures of coated membrane vesicles have not been obtained. Here, we solved the structures of individual COPI-coated membrane vesicles by cryoelectron tomography and subtomogram averaging of in vitro reconstituted budding reactions. The coat protein complex, coatomer, was observed to adopt alternative conformations to change the number of other coatomers with which it interacts and to form vesicles with variable sizes and shapes. This represents a fundamentally different basis for vesicle coat assembly.

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Language(s): eng - English
 Dates: 2012
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000305211700049
DOI: 10.1126/science.1221443
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: 336 (6087) Sequence Number: - Start / End Page: 1451 - 1454 Identifier: -