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Coat formation in coated vesicles.

K Prasad, R E Lippoldt, H Edelhoch

    Biochemistry
    |November 5, 1985
    PubMed
    Summary
    This summary is machine-generated.

    Coat proteins (100,000-110,000 Mr) facilitate clathrin polymerization and uniform basket formation. These proteins are crucial for binding clathrin to uncoated vesicles, forming coated vesicles efficiently.

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    Area of Science:

    • Cell Biology
    • Protein Biochemistry

    Background:

    • Coated vesicles are essential for intracellular transport.
    • Clathrin forms the structural coat of these vesicles.
    • The role of accessory proteins in coat assembly is not fully understood.

    Purpose of the Study:

    • To investigate the role of 100,000-110,000 Mr coat proteins in clathrin assembly.
    • To determine the importance of these proteins in the formation of coated vesicles.

    Main Methods:

    • Preparation of 100,000-110,000 Mr coat proteins using two distinct methods.
    • Fluorescent labeling of clathrin, coat proteins, and uncoated vesicles.
    • Analysis of component distribution on sucrose gradients.

    Main Results:

    Related Experiment Videos

    • The 100,000-110,000 Mr coat proteins promote homogeneous, small-size clathrin basket formation.
    • These proteins significantly increase the rate of clathrin polymerization.
    • The coat proteins are vital for the binding of clathrin to uncoated vesicles.

    Conclusions:

    • The 100,000-110,000 Mr proteins are key regulators of clathrin coat assembly.
    • Efficient formation of coated vesicles relies on these accessory proteins.