Structure and organization of coat proteins in the COPII cage

Cell. 2007 Jun 29;129(7):1325-36. doi: 10.1016/j.cell.2007.05.036.

Abstract

COPII-coated vesicles export newly synthesized proteins from the endoplasmic reticulum. The COPII coat consists of the Sec23/24-Sar1 complex that selects cargo and the Sec13/31 assembly unit that can polymerize into an octahedral cage and deform the membrane into a bud. Crystallographic analysis of the assembly unit reveals a 28 nm long rod comprising a central alpha-solenoid dimer capped by two beta-propeller domains at each end. We construct a molecular model of the COPII cage by fitting Sec13/31 crystal structures into a recently determined electron microscopy density map. The vertex geometry involves four copies of the Sec31 beta-propeller that converge through their axial ends; there is no interdigitation of assembly units of the kind seen in clathrin cages. We also propose that the assembly unit has a central hinge-an arrangement of interlocked alpha-solenoids-about which it can bend to adapt to cages of variable curvature.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COP-Coated Vesicles / chemistry*
  • COP-Coated Vesicles / ultrastructure*
  • Cells, Cultured
  • Clathrin / metabolism
  • Crystallography, X-Ray
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / ultrastructure
  • Golgi Apparatus / metabolism
  • Golgi Apparatus / ultrastructure
  • Macromolecular Substances
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / metabolism
  • Protein Structure, Secondary / physiology
  • Protein Structure, Tertiary / physiology
  • Protein Transport / physiology
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Vesicular Transport Proteins / chemistry*
  • Vesicular Transport Proteins / metabolism

Substances

  • Clathrin
  • Macromolecular Substances
  • Membrane Proteins
  • Nuclear Pore Complex Proteins
  • SEC13 protein, S cerevisiae
  • SEC31 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins