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Dynamin-mediated internalization of caveolae

J R Henley1, E W Krueger, B J Oswald

  • 1Department of Molecular Neuroscience, Mayo Clinic, Rochester, Minnesota 55905, USA.

The Journal of Cell Biology
|May 16, 1998
PubMed
Summary
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Dynamin II protein is crucial for cellular uptake, mediating both clathrin-mediated endocytosis and caveolae internalization in mammalian cells. This research clarifies dynamin

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Dynamins are GTPases involved in endocytosis.
  • The specific roles of dynamin isoforms, like dynamin II, in mammalian epithelial cells remain unclear.
  • Understanding dynamin II function is key to deciphering distinct endocytic pathways.

Purpose of the Study:

  • To define the function of dynamin II in mammalian epithelial cells.
  • To investigate dynamin II's role in both clathrin-dependent and non-clathrin-dependent endocytosis.
  • To elucidate the involvement of dynamin II in caveolae internalization.

Main Methods:

  • Generation and characterization of peptide-specific antibodies against dynamin II.
  • Microinjection of antibodies into cultured hepatocytes.

Related Experiment Videos

  • Analysis of endocytic processes using microscopy and immunoisolation techniques.
  • Immunofluorescence microscopy to assess protein colocalization.

    • Main Results:

    • Dynamin II antibodies inhibited clathrin-mediated endocytosis.
    • Antibody injection induced formation of long plasmalemmal invaginations with coated pits.
    • Accumulation of flask-shaped invaginations resembling caveolae observed.
    • Caveolae-mediated endocytosis of cholera toxin B was inhibited.
    • Dynamin was biochemically isolated with caveolar membranes.
    • Dynamin colocalized with caveolin, a caveolar coat protein.

    Conclusions:

    • Dynamin II plays a critical role in mammalian cell endocytosis.
    • Dynamin II mediates both clathrin-dependent endocytosis and caveolae internalization.
    • These findings highlight dynamin II's dual function in distinct cellular uptake pathways.