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

被引：68

作者：

Faini, Marco ^{[1
]}

Prinz, Simone ^{[1
]}

Beck, Rainer ^{[2
]}

Schorb, Martin ^{[1
]}

Riches, James D. ^{[1
]}

Bacia, Kirsten ^{[3
]}

Brugger, Britta ^{[2
]}

Wieland, Felix T. ^{[2
]}

Briggs, John A. G. ^{[1
,4
]}

机构：

[1] European Mol Biol Lab, Struct & Computat Biol Unit, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

[2] Heidelberg Univ Biochem Ctr, Univ Heidelberg, Neuenheimer Feld 328, D-69120 Heidelberg, Germany

[3] Univ Halle, HALOmem, Kurt Mothes Strasse 3, D-06120 Halle, Germany

[4] European Mol Biol Lab, Cell Biol & Biophys Unit, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

来源：

SCIENCE | 2012年 / 336卷 / 6087期

关键词：

CRYOELECTRON TOMOGRAPHY; CLATHRIN; TRANSPORT; COMPLEXES; MECHANISM; CAGE;

D O I：

10.1126/science.1221443

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1451 / +

页数：5

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