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Structural basis for cargo regulation of COPII coat assembly.

ABSTRACT: Using cryo-electron microscopy, we have solved the structure of an icosidodecahedral COPII coat involved in cargo export from the endoplasmic reticulum (ER) coassembled from purified cargo adaptor Sec23-24 and Sec13-31 lattice-forming complexes. The coat structure shows a tetrameric assembly of the Sec23-24 adaptor layer that is well positioned beneath the vertices and edges of the Sec13-31 lattice. Fitting the known crystal structures of the COPII proteins into the density map reveals a flexible hinge region stemming from interactions between WD40 beta-propeller domains present in Sec13 and Sec31 at the vertices. The structure shows that the hinge region can direct geometric cage expansion to accommodate a wide range of bulky cargo, including procollagen and chylomicrons, that is sensitive to adaptor function in inherited disease. The COPII coat structure leads us to propose a mechanism by which cargo drives cage assembly and membrane curvature for budding from the ER.

SUBMITTER: Stagg SM

PROVIDER: S-EPMC2649882 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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Structural basis for cargo regulation of COPII coat assembly.

Stagg Scott M SM LaPointe Paul P Razvi Abbas A Gürkan Cemal C Potter Clinton S CS Carragher Bridget B Balch William E WE

Cell 20080801 3

Using cryo-electron microscopy, we have solved the structure of an icosidodecahedral COPII coat involved in cargo export from the endoplasmic reticulum (ER) coassembled from purified cargo adaptor Sec23-24 and Sec13-31 lattice-forming complexes. The coat structure shows a tetrameric assembly of the Sec23-24 adaptor layer that is well positioned beneath the vertices and edges of the Sec13-31 lattice. Fitting the known crystal structures of the COPII proteins into the density map reveals a flexibl ...[more]

PMID: 18692470

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Structural basis of cargo membrane protein discrimination by the human COPII coat machinery.

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