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Structural basis for cargo regulation of COPII coat assembly

Academic Article
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Overview

authors

  • Stagg, S. M.
  • LaPointe, P.
  • Razvi, A.
  • Gurkan, C.
  • Potter, Clinton
  • Carragher, Bridget
  • Balch, William E.

publication date

  • August 2008

journal

  • Cell  Journal

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.

subject areas

  • Carrier Proteins
  • Cryoelectron Microscopy
  • Endoplasmic Reticulum
  • Humans
  • Models, Molecular
  • Protein Transport
  • Vesicular Transport Proteins
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Identity

PubMed Central ID

  • PMC2649882

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2008.06.024

PubMed ID

  • 18692470
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Additional Document Info

start page

  • 474

end page

  • 484

volume

  • 134

issue

  • 3

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