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Related Experiment Videos

Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network.

Pradipta Ghosh1, Stuart Kornfeld

  • 1Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

The Journal of Biological Chemistry
|February 13, 2003
PubMed
Summary

Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding (GGA) proteins regulate cell transport. GGA1 protein activity is controlled by phosphorylation, with dephosphorylation enabling its membrane binding and cargo transport at the Golgi.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding (GGA) proteins are crucial for intracellular protein transport.
  • GGAs mediate cargo packaging into clathrin-coated vesicles at the trans-Golgi network.
  • The precise regulation of GGA function remains an active area of research.

Purpose of the Study:

  • To investigate the regulatory mechanisms governing the function of GGA1, a key protein in intracellular transport.
  • To elucidate the role of phosphorylation and dephosphorylation in GGA1 activity.
  • To understand how GGA1 interacts with other proteins and membranes.

Main Methods:

  • Cell fractionation to localize phosphorylated GGA1.
  • Inhibition studies using okadaic acid and in vitro dephosphorylation assays.

Related Experiment Videos

  • Biophysical analyses including gel filtration and sucrose gradient centrifugation to assess conformational changes.

    • Main Results:

    • Phosphorylated GGA1 predominantly resides in the cytosol.
    • Recruitment of GGA1 to membranes is coupled with its dephosphorylation.
    • Dephosphorylation by a protein phosphatase 2A-like enzyme induces an 'open' conformation in GGA1.
    • This conformational change enhances GGA1 binding to ligands and the adaptor protein complex-1 gamma-appendage.

    Conclusions:

    • GGA1 function is dynamically regulated by phosphorylation and dephosphorylation cycles.
    • Dephosphorylation activates GGA1 by promoting a conformational change that enhances its binding capabilities.
    • A model for GGA1 regulation at the trans-Golgi network involving these post-translational modifications is proposed.