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TitleStructural basis for cargo regulation of COPII coat assembly.
Journal, issue, pagesCell, Vol. 134, Issue 3, Page 474-484, Year 2008
Publish dateAug 8, 2008
AuthorsScott M Stagg / Paul LaPointe / Abbas Razvi / Cemal Gürkan / Clinton S Potter / Bridget Carragher / William E Balch /
PubMed AbstractUsing 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 ...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.
External linksCell / PubMed:18692470 / PubMed Central
MethodsEM (single particle)
Resolution43.0 Å
Structure data

EMDB-1511:
COPII coat
Method: EM (single particle) / Resolution: 43.0 Å

Source
  • Homo sapiens (human)

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