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Lee, Changwook
Structural Biology of Cellular Biochemistry Lab
Research Interests
  • Cell biology, structural biology, protein biochemistry, membrane biology, cancer biology

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Structure of Coatomer Cage Proteins and the Relationship among COPI, COPII, and Clathrin Vesicle Coats

Cited 69 times inthomson ciCited 65 times inthomson ci
Title
Structure of Coatomer Cage Proteins and the Relationship among COPI, COPII, and Clathrin Vesicle Coats
Author
Lee, ChangwookGoldberg, Jonathan
Keywords
Cellbio; Proteins
Issue Date
2010-07
Publisher
CELL PRESS
Citation
CELL, v.142, no.1, pp.123 - 132
Abstract
COPI-coated vesicles form at the Golgi apparatus from two cytosolic components, ARF G protein and coatomer, a heptameric complex that can polymerize into a cage to deform the membrane into a bud. Although coatomer shares a common evolutionary origin with COPII and clathrin vesicle coat proteins, the architectural relationship among the three cages is unclear. Strikingly, the αβ'-COP core of coatomer crystallizes as a triskelion in which three copies of a β'-COP β-propeller domain converge through their axial ends. We infer that the trimer constitutes the vertex of the COPI cage. Our model proposes that the COPI cage is intermediate in design between COPII and clathrin: COPI shares with clathrin an arrangement of three curved α-solenoid legs radiating from a common center, and COPI shares with COPII highly similar vertex interactions involving the axial ends of β-propeller domains.
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DOI
10.1016/j.cell.2010.05.030
ISSN
0092-8674
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BME_Journal Papers
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