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Dynamin GTPase, a force-generating molecular switch

D E Warnock1, S L Schmid

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

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|November 1, 1996
PubMed
Summary
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Dynamin, a GTPase, acts as a structural protein in clathrin-coated vesicle formation. Its GTP hydrolysis drives vesicle detachment by tightening a collar-like structure, revealing a mechano-chemical function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Dynamin is a GTPase crucial for clathrin-coated vesicle formation.
  • It plays a role in the late stages of endocytosis.

Purpose of the Study:

  • To elucidate the mechanism by which dynamin regulates vesicle detachment.
  • To explore dynamin's function as a mechano-chemical protein.

Main Methods:

  • The study likely involved biochemical assays and structural analyses to understand dynamin's GTPase activity and oligomerization.
  • Observational studies of vesicle formation in cells may have been employed.

Main Results:

  • Dynamin assembles into a collar around invaginated coated pit necks.

Related Experiment Videos

  • GTP hydrolysis induces a conformational change, tightening the collar and promoting vesicle detachment.
  • Dynamin exhibits unique properties: low GTP affinity, high GTPase activity, and homo-oligomerization.

    • Conclusions:

    • Dynamin functions as a structural protein with mechano-chemical properties, distinct from typical GTPase molecular switches.
    • Coordinated GTP hydrolysis within the dynamin oligomer generates the force required for vesicle scission.