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Related Experiment Videos

Dynamin self-assembly stimulates its GTPase activity

D E Warnock1, J E Hinshaw, S L Schmid

  • 1Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

The Journal of Biological Chemistry
|September 13, 1996
PubMed
Summary
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Dynamin self-assembly significantly enhances its GTPase activity, identifying dynamin as a key physiological regulator. This cycle of assembly, GTP hydrolysis, and disassembly drives vesicle budding.

Area of Science:

  • Molecular and Cell Biology
  • Biochemistry
  • Membrane Trafficking

Background:

  • Dynamin (a GTPase) is crucial for coated vesicle budding from the plasma membrane.
  • Various molecules like microtubules stimulate dynamin's GTPase activity in vitro, but physiological relevance is unclear.
  • Dynamin self-assembles into ring-like structures, particularly around microtubules, resembling in vivo structures.

Purpose of the Study:

  • To investigate the role of dynamin self-assembly in regulating its GTPase activity.
  • To identify physiologically relevant effectors of dynamin GTPase activity.

Main Methods:

  • Studied purified dynamin self-assembly under low ionic strength conditions.
  • Measured GTPase activity of assembled dynamin.
  • Utilized a GTP-binding and hydrolysis-defective dynamin mutant in co-assembly experiments.

Related Experiment Videos

  • Observed the effect of GTP on dynamin assembly structures.

    • Main Results:

    • Dynamin self-assembly stimulates its GTPase activity up to 10-fold.
    • Dynamin itself is identified as the first physiologically relevant effector of its GTPase activity.
    • Stimulated GTPase activity of assembled dynamin does not require direct high-affinity GTP binding site interaction.
    • GTP destabilizes assembled dynamin structures, indicating a dynamic assembly-hydrolysis-disassembly cycle.

    Conclusions:

    • Dynamin self-assembly is a critical mechanism for regulating its GTPase activity.
    • The dynamic cycle of dynamin assembly, GTP hydrolysis, and disassembly is essential for vesicle budding.
    • Dynamin acts as a key regulator of its own GTPase activity in a physiological context.