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Related Experiment Videos

A kinetic proof-reading mechanism for protein sorting.

Matthias Weiss1, Tommy Nilsson

  • 1Cell Biology and Cell Biophysics Programme, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. mweiss@embl-heidelberg.de

Traffic (Copenhagen, Denmark)
|February 1, 2003
PubMed
Summary

Resident proteins are sorted via coatomer protein I (COPI) recycling, requiring ADP-ribosylation factor 1 (ARF-1) GTP hydrolysis. A new kinetic model explains how cargo-induced ARFGAP1 sequestration drives efficient COPI-mediated protein sorting.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Proteins in the exocytic pathway are regulated by coatomer protein I (COPI)-mediated recycling.
  • Sorting of cargo by COPI depends on GTP hydrolysis by ADP-ribosylation factor 1 (ARF-1).
  • ARF-1 recruits coatomer to Golgi membranes, and its hydrolysis releases coatomer into the cytosol, a process requiring ARFGAP1.

Purpose of the Study:

  • To formulate a kinetic proof-reading model for COPI-mediated protein sorting.
  • To explain how GTP hydrolysis-driven coat release results in active sorting.
  • To investigate the role of ARFGAP1 in coupling cargo sorting to coat release.

Main Methods:

  • Development of a kinetic proof-reading model.
  • Incorporation of cargo-induced ARFGAP1 sequestration into the model.

Related Experiment Videos

  • Analysis of GTP hydrolysis-driven coat release dynamics.

    • Main Results:

    • The model explains how GTP hydrolysis can drive active sorting events.
    • The model predicts a dependency of sorting efficiency on ARFGAP1 concentration.
    • The model accounts for differential detachment kinetics of ARF-1 and COPI from Golgi membranes in vivo.

    Conclusions:

    • A kinetic proof-reading model successfully explains COPI-mediated protein sorting.
    • Cargo-induced ARFGAP1 sequestration is a key mechanism for efficient sorting.
    • The model provides a framework for understanding the dynamics of COPI-mediated transport.