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Gamma-COP appendage domain - structure and function.

Peter J Watson1, Gabriella Frigerio, Brett M Collins

  • 1Cambridge Institute for Medical Research & Department of Clinical Biochemistry, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK.

Traffic (Copenhagen, Denmark)
|December 24, 2003
PubMed
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The COPI coat complex facilitates vesicle transport between cellular compartments. Researchers elucidated the structure of gamma-COP, revealing a key binding site for ARFGAP proteins involved in this transport process.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • COPI-coated vesicles are crucial for retrograde transport from the Golgi to the ER and intra-Golgi transport.
  • The COPI coat is formed by the heptameric coatomer complex, comprising two distinct subcomplexes.

Purpose of the Study:

  • To determine the structure of the appendage domain of gamma-COP.
  • To identify protein interaction sites on the gamma-COP appendage and their functional relevance.

Main Methods:

  • X-ray crystallography to determine the structure of the gamma-COP appendage domain.
  • Site-directed mutagenesis and protein-protein interaction assays in yeast and mammalian systems.

Main Results:

  • The gamma-COP appendage domain shares structural similarity with the alpha-appendage of AP2, featuring a protein/protein interaction site.

Related Experiment Videos

  • This site binds to ARFGAP proteins: Glo3p in yeast and ARFGAP2 in mammals.
  • Mutational analysis suggests a second binding site on the gamma-COP appendage for the alpha, beta', epsilon-COP subcomplex.

    • Conclusions:

    • The structure of the gamma-COP appendage reveals conserved features with clathrin adaptors.
    • The identified binding sites are critical for regulating COPI vesicle formation and function.
    • This work provides insights into the molecular mechanisms governing retrograde transport in eukaryotic cells.