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Related Experiment Videos

Multiple distinct coiled-coils are involved in dynamin self-assembly.

P M Okamoto1, B Tripet, J Litowski

  • 1Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.

The Journal of Biological Chemistry
|April 3, 1999
PubMed
Summary

Dynamin self-assembly involves two C-terminal coiled-coil domains, crucial for membrane scission in endocytosis. These domains mediate interactions between dynamin isoforms and influence GTPase mutant inhibition.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Dynamin, a GTPase, is vital for membrane trafficking processes like endocytosis.
  • Dynamin self-assembles into polymers, forming helical structures around membrane invaginations.
  • Understanding dynamin's self-assembly is key to elucidating its role in membrane scission.

Purpose of the Study:

  • To identify and characterize the self-assembly regions within dynamin.
  • To investigate the structural basis of dynamin oligomerization.
  • To understand how self-assembly domains affect dynamin function and interactions.

Main Methods:

  • Co-immunoprecipitation and yeast interaction trap assays to assess self-association.
  • Sedimentation analysis to determine oligomeric states.

Related Experiment Videos

  • Circular dichroism spectroscopy and equilibrium ultracentrifugation of peptides to study coiled-coil formation and oligomerization.

    • Main Results:

    • Deletion of C-terminal sequences abolished dynamin self-association and reduced sedimentation.
    • Peptide analysis revealed coiled-coil formation in C-terminal and central domains.
    • Two peptides formed tetramers, suggesting roles in monomer-tetramer transitions.
    • C-terminal domain deletions reversed endocytic inhibition by dynamin mutants.
    • Interactions were observed between different dynamin isoforms.

    Conclusions:

    • Dynamin possesses two distinct coiled-coil assembly domains.
    • These domains mediate self-association, including interactions between isoforms.
    • The findings support a parallel model for dynamin subunit assembly.
    • Self-assembly is critical for dynamin's role in endocytosis and regulating GTPase activity.