DOI: 10.1126/science.1221443. The Structures of COPI-Coated Vesicles Reveal Alternate Coatomer Conformations and Interactions

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

10.1126/science.1221443

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

COPy Coat COPI-coated vesicles are responsible for intracellular vesicular transport both within the Golgi and between the Golgi and endoplasmic reticulum. By applying subtomogram averaging from cryoelectron tomography data, Faini et al. (p. 1451 , published online 24 May) were able to describe the complete three-dimensional structure for COPI-coated vesicles generated in a cell-free, membrane-budding reaction. The structures of multiple individual vesicles reveal assembly principles based on interactions that, unlike those for clathrin-coated vesicles, are not regular: The basic subunit can undergo significant conformational changes and assemble with different stoichiometries. This variability may allow the regulation of membrane curvature and vesicle size. Furthermore, forming a complete closed coat was not required to produce budded vesicles.

Bibliography

Faini, M., Prinz, S., Beck, R., Schorb, M., Riches, J. D., Bacia, K., BrÃ¼gger, B., Wieland, F. T., & Briggs, J. A. G. (2012). The Structures of COPI-Coated Vesicles Reveal Alternate Coatomer Conformations and Interactions. Science, 336(6087), 1451â1454.

Authors 9

Marco Faini (first)
Simone Prinz (additional)
Rainer Beck (additional)
Martin Schorb (additional)
James D. Riches (additional)
Kirsten Bacia (additional)
Britta Brügger (additional)
Felix T. Wieland (additional)
John A. G. Briggs (additional)

References 30 Referenced 74

Dates

Type	When
Created	13 years, 3 months ago (May 25, 2012, 7:01 a.m.)
Deposited	1 year, 7 months ago (Jan. 10, 2024, 8:59 a.m.)
Indexed	3 weeks, 4 days ago (Aug. 1, 2025, 11:58 p.m.)
Issued	13 years, 2 months ago (June 15, 2012)
Published	13 years, 2 months ago (June 15, 2012)
Published Print	13 years, 2 months ago (June 15, 2012)

Funders 0

None

BibTeX

@article{Faini_2012, title={The Structures of COPI-Coated Vesicles Reveal Alternate Coatomer Conformations and Interactions}, volume={336}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1221443}, DOI={10.1126/science.1221443}, number={6087}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Faini, Marco and Prinz, Simone and Beck, Rainer and Schorb, Martin and Riches, James D. and Bacia, Kirsten and Brügger, Britta and Wieland, Felix T. and Briggs, John A. G.}, year={2012}, month=jun, pages={1451–1454} }

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  "abstract": "<jats:title>COPy Coat</jats:title>\n          <jats:p>\n            COPI-coated vesicles are responsible for intracellular vesicular transport both within the Golgi and between the Golgi and endoplasmic reticulum. By applying subtomogram averaging from cryoelectron tomography data,\n            <jats:bold>\n              Faini\n              <jats:italic>et al.</jats:italic>\n            </jats:bold>\n            (p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"1451\" related-article-type=\"in-this-issue\" vol=\"336\" xlink:href=\"10.1126/science.1221443\">1451</jats:related-article>\n            , published online 24 May) were able to describe the complete three-dimensional structure for COPI-coated vesicles generated in a cell-free, membrane-budding reaction. The structures of multiple individual vesicles reveal assembly principles based on interactions that, unlike those for clathrin-coated vesicles, are not regular: The basic subunit can undergo significant conformational changes and assemble with different stoichiometries. This variability may allow the regulation of membrane curvature and vesicle size. Furthermore, forming a complete closed coat was not required to produce budded vesicles.\n          </jats:p>",
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