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Bending a membrane: how clathrin affects budding.

Lars Hinrichsen1, Anika Meyerholz, Stephanie Groos

  • 1Department of Cell Biology, Center of Anatomy, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625 Hannover, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|June 1, 2006
PubMed
Summary
This summary is machine-generated.

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Clathrin is essential for endocytosis, driving membrane invagination. Even without clathrin, adapter protein domains persist but lack curvature, indicating clathrin

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Receptor-mediated endocytosis is a crucial cellular process for ligand uptake.
  • Clathrin is a key protein involved in forming coated vesicles for endocytosis.
  • Adapter protein complexes like AP2 and accessory proteins (CALM, epsin, eps15/eps15R) are recruited to the plasma membrane during endocytosis.

Purpose of the Study:

  • To investigate the role of clathrin in the formation and dynamics of endocytic domains.
  • To characterize membrane domains containing AP2 and accessory proteins in clathrin-depleted cells.
  • To elucidate the mechanism by which clathrin drives coated pit invagination.

Main Methods:

  • RNA interference was used to block clathrin synthesis in HeLa cells.

Related Experiment Videos

  • Fluorescence microscopy and electron microscopy were employed to analyze membrane domain characteristics.
  • Fluorescence recovery after photobleaching (FRAP) was used to assess protein dynamics.

    • Main Results:

    • Clathrin depletion suppressed receptor-mediated endocytosis but did not eliminate AP2-coated vesicle adapter and accessory protein domains at the plasma membrane.
    • These domains persisted, showing similar size and number to those in clathrin-expressing cells, with no significant change in AP2 molecule exchange rates.
    • Electron microscopy revealed that AP2 membrane domains lacked curvature, and their dispersion occurred upon disruption of protein-protein interactions involving the AP2 alpha appendage domain.

    Conclusions:

    • Clathrin is essential for driving the invagination of coated pits during endocytosis.
    • AP2 and associated proteins can form stable membrane domains independently of clathrin.
    • A 'Brownian ratchet' mechanism is proposed to be consistent with clathrin-mediated coated vesicle formation.