Literature DB >> 26160949

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

S O Dodonova1, P Diestelkoetter-Bachert2, A von Appen1, W J H Hagen1, R Beck2, M Beck1, F Wieland2, J A G Briggs3.   

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.
Copyright © 2015, American Association for the Advancement of Science.

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Year:  2015        PMID: 26160949     DOI: 10.1126/science.aab1121

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  80 in total

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4.  9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.

Authors:  Svetlana O Dodonova; Patrick Aderhold; Juergen Kopp; Iva Ganeva; Simone Röhling; Wim J H Hagen; Irmgard Sinning; Felix Wieland; John A G Briggs
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Review 9.  Sphingolipids and lipid rafts: Novel concepts and methods of analysis.

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