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Related Experiment Videos

Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape.

M A McNiven1, L Kim, E W Krueger

  • 1Department of Biochemistry and Molecular Biology, Center for Basic Research in Digestive Diseases, Mayo Clinic, Rochester, Minnesota 55905, USA.

The Journal of Cell Biology
|October 6, 2000
PubMed
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Dynamin, a GTPase involved in vesicle formation, interacts with the actin-binding protein cortactin. This interaction influences cell shape and actin reorganization during cell migration.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Dynamin GTPases are crucial for vesicle formation in endocytic and secretory pathways.
  • The actin cytoskeleton influences cell shape, migration, endocytosis, and secretion.
  • Dynamin and actin cytoskeleton interactions are postulated to be synergistic.

Purpose of the Study:

  • To investigate the dynamic changes in dynamin distribution during cell migration.
  • To elucidate the molecular mechanisms underlying dynamin's interaction with the actin cytoskeleton.
  • To determine the functional consequences of dynamin-cortactin interaction on cell morphology and actin organization.

Main Methods:

  • Immunofluorescence microscopy and GFP-tagging to visualize dynamin localization.

Related Experiment Videos

  • Biochemical assays to confirm protein-protein interactions.
  • Expression of wild-type and mutant dynamin and cortactin in cultured fibroblasts.

    • Main Results:

    • Dynamin 2 (Dyn 2) localization shifts from vesicles to membrane ruffles and lamellipodia upon PDGF-induced cell migration.
    • Dynamin interacts with cortactin via its proline-rich domain (PRD) and cortactin's SH3 domain.
    • Altered expression of cortactin or dynamin mutants affects dynamin recruitment to ruffles and leads to significant changes in cell morphology, including increased actin stress fibers.

    Conclusions:

    • Dynamin interacts with the actin cytoskeleton through cortactin.
    • This interaction plays a role in regulating actin reorganization and cell shape.
    • The findings reveal a novel mechanism linking dynamin function to actin dynamics and cell morphology.