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Related Experiment Videos

AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin.

W Hao1, Z Luo, L Zheng

  • 1Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245, USA.

The Journal of Biological Chemistry
|July 31, 1999
PubMed
Summary

The interaction between AP180 and AP-2 proteins directly enhances clathrin assembly for vesicle trafficking. Phosphorylation of AP180 regulates this interaction, controlling clathrin vesicle dynamics in cells.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Clathrin-coated vesicles mediate intracellular protein and lipid transport.
  • AP-2 and AP180 are key coat proteins in nerve terminal clathrin-coated vesicles.
  • Efficient clathrin assembly by AP-2 and AP180 is pH-dependent, failing at physiological pH.

Purpose of the Study:

  • To investigate the direct interaction between AP180 and AP-2.
  • To determine how this interaction affects clathrin assembly under physiological conditions.
  • To elucidate the role of AP180 phosphorylation in regulating this interaction and vesicle dynamics.

Main Methods:

  • Investigated direct, clathrin-independent interaction between AP180 and AP-2.
  • Assessed clathrin assembly efficiency of AP180-AP-2 complexes at physiological pH.

Related Experiment Videos

  • Examined the effect of AP180 phosphorylation by casein kinase II in vitro and in vivo.
  • Localized the AP-2 binding site on AP180 using recombinant protein fragments.

    • Main Results:

    • The AP180-AP-2 complex shows enhanced clathrin assembly at physiological pH compared to individual proteins.
    • AP180 phosphorylation by casein kinase II weakens AP-2 binding and cooperative clathrin assembly.
    • The AP-2 binding site on AP180 was mapped to amino acids 623-680.
    • A fragment containing the AP-2 binding site disrupted the AP180-AP-2 complex and its clathrin assembly activity.

    Conclusions:

    • AP180 and AP-2 directly interact to form a complex that efficiently assembles clathrin.
    • AP180 phosphorylation modulates AP-2 binding affinity, suggesting a regulatory mechanism for clathrin assembly in vivo.
    • This interaction and its regulation are crucial for clathrin-coated vesicle dynamics.