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Related Experiment Videos

Brain clathrin and clathrin-associated proteins

M P Lisanti, W Schook, N Moskowitz

    The Biochemical Journal
    |February 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

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    Clathrin-associated proteins (CAPs) are essential for forming clathrin baskets in vitro. Removing these proteins prevents basket assembly, indicating their crucial role in clathrin structure.

    Area of Science:

    • Cell Biology
    • Structural Biology
    • Biochemistry

    Background:

    • Clathrin self-assembles into baskets or cages, a process critical for vesicle formation.
    • The precise molecular requirements for clathrin basket assembly in vitro are not fully understood.

    Purpose of the Study:

    • To investigate the role of associated proteins in clathrin assembly.
    • To identify the specific components necessary for in vitro clathrin basket formation.

    Main Methods:

    • Isolation of clathrin and associated proteins from bovine brain coated vesicles.
    • Sepharose 4B column chromatography to separate clathrin from associated proteins.
    • Limited proteolysis and enzymatic treatment to remove clathrin-associated proteins (CAPs).

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    Main Results:

    • Clathrin eluted with a 30,000-mol.wt. doublet retained the ability to form baskets at pH 6.5.
    • Limited proteolysis removed CAPs, yielding clathrin that assembled into open lattices but not baskets.
    • Enzymatic cleavage of CAPs from coated vesicles and baskets confirmed their surface localization.

    Conclusions:

    • A polypeptide doublet (30,000-mol.wt.) is crucial for clathrin basket assembly.
    • Clathrin-associated proteins (CAPs) are external components required for proper clathrin cage formation.
    • These findings elucidate the structural requirements for clathrin assembly in vitro.