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

• Published in: Cell Vol. 142; no. 1; pp. 123 - 132
• Main Authors: Lee, Changwook, Goldberg, Jonathan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 09.07.2010
• Subjects: Amino Acid Sequence; Animals; BASIC BIOLOGICAL SCIENCES; Cattle; CELLBIO; Clathrin - metabolism; Coat Protein Complex I - chemistry; Coat Protein Complex I - metabolism; Coatomer Protein - chemistry; COP-Coated Vesicles - chemistry; COP-Coated Vesicles - metabolism; Crystallography, X-Ray; DESIGN; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; GOLGI COMPLEXES; LEGS; MEMBRANES; Models, Molecular; Molecular Sequence Data; ORIGIN; Protein Structure, Tertiary; PROTEINS; Sequence Alignment; CELLBIO; PROTEINS
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/j.cell.2010.05.030

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. [Display omitted] ► Crystal structures of αβ′-COP and αɛ-COP subcomplexes of the COPI vesicular cage ► The αβ′-COP subcomplex forms a triskelion ► COPI cage shares architectural features with both clathrin and COPII vesicular cages