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Related Experiment Videos

Complex formation between clathrin and uncoating ATPase

K Prasad1, J Heuser, E Eisenberg

  • 1Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.

The Journal of Biological Chemistry
|March 4, 1994
PubMed
Summary
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Bovine brain uncoating ATPase (a heat shock protein) interacts with clathrin. ATP facilitates complex formation and dissociation, while ADP inhibits these processes, revealing a single nucleotide-binding site.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Clathrin-coated vesicles are essential for intracellular trafficking.
  • Uncoating ATPase is a 70-kDa heat shock protein involved in vesicle uncoating.

Purpose of the Study:

  • To investigate the interaction between bovine brain uncoating ATPase and clathrin.
  • To elucidate the role of ATP and ADP in the uncoating ATPase-clathrin complex formation and dissociation.

Main Methods:

  • Comparison of uncoating ATPase-clathrin complexes formed via uncoating reaction versus direct binding.
  • Analysis of complex formation kinetics and stoichiometry.
  • Electron microscopy to visualize complex structure and binding sites.

Main Results:

Related Experiment Videos

  • Uncoating ATPase forms a single type of complex with clathrin, with a 1:1 stoichiometry of ATPase to clathrin heavy chain.
  • ATP accelerates complex formation and dissociation, whereas ADP inhibits these rates.
  • ADP binding to the single nucleotide site prevents complex formation/dissociation, while ATP binding promotes rapid formation/dissociation.

Conclusions:

  • Bovine brain uncoating ATPase interacts with clathrin through a single nucleotide-binding site.
  • The ATPase's activity is regulated by ATP/ADP binding, controlling clathrin complex dynamics.