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Related Experiment Videos

A model for dynamin self-assembly based on binding between three different protein domains.

E Smirnova1, D L Shurland, E D Newman-Smith

  • 1Department of Biological Chemistry, University of California, Los Angeles, California 90095-1737, USA.

The Journal of Biological Chemistry
|May 18, 1999
PubMed
Summary
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Dynamin self-assembly into spirals involves three key intramolecular binding interactions. These interactions, including dimerization and nucleotide-state-dependent binding, explain how dynamin forms functional structures for vesicle budding.

Area of Science:

  • Biochemistry
  • Cell Biology

Background:

  • Dynamin is a GTPase crucial for clathrin-coated vesicle formation.
  • Understanding dynamin's self-assembly mechanism is key to elucidating its role in endocytosis.

Purpose of the Study:

  • To identify and characterize the intramolecular binding interactions driving dynamin self-assembly.
  • To propose a model for dynamin multimerization based on these interactions.

Main Methods:

  • Analysis of intramolecular binding interactions within dynamin.
  • Site-directed mutagenesis to probe GTP binding motifs.
  • In vitro binding experiments to assess domain interactions.

Main Results:

  • Identified three distinct intramolecular binding interactions in dynamin.

Related Experiment Videos

  • The C-terminal assembly domain mediates dimerization and interacts with the N-terminal GTPase and middle domains.
  • GTP binding state regulates the interaction between the assembly domain and GTPase domain.

    • Conclusions:

    • Dynamin self-assembly proceeds via dimerization of the assembly domain.
    • Subsequent interactions link dimers and potentially form spiral rungs, regulated by GTP binding.
    • These findings provide a molecular basis for dynamin's role in vesicle dynamics.