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Effect of basic compounds on the polymerization of clathrin

P K Nandi, P P Van Jaarsveld, R E Lippoldt

    Biochemistry
    |November 10, 1981
    PubMed
    Summary

    Divalent cations like Ca2+ and Mn2+, spermine, and lysozyme significantly accelerate clathrin polymerization. These compounds enable clathrin coat formation at physiological pH, crucial for cellular processes.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Structural Biology

    Background:

    • Clathrin self-assembles into 300S coat structures, essential for protein trafficking.
    • Clathrin polymerization typically requires acidic pH (≤6.8) for efficient assembly.
    • Understanding factors that regulate clathrin assembly is vital for cellular function.

    Purpose of the Study:

    • To investigate the effects of divalent cations, polybasic amines, and basic proteins on clathrin polymerization rates.
    • To identify compounds that can promote clathrin assembly at physiological pH.

    Main Methods:

    • Turbidimetric assays were employed to measure the rate of clathrin polymerization.
    • The influence of various divalent cations (e.g., Ca2+, Mn2+), polybasic amines (e.g., spermine), and proteins (e.g., lysozyme) was assessed.

    Main Results:

    • Calcium (Ca2+) and manganese (Mn2+) ions strongly enhanced clathrin polymerization rates.
    • Spermine was the most effective naturally occurring polybasic amine in promoting polymerization.
    • Lysozyme significantly stimulated the rate of clathrin assembly.
    • Several tested compounds facilitated clathrin polymerization at physiological pH (around 7.4).

    Conclusions:

    • Specific divalent cations, polyamines, and basic proteins can act as potent stimulators of clathrin polymerization.
    • These findings suggest potential mechanisms for regulating clathrin coat formation in vivo.
    • The ability to induce polymerization at physiological pH has implications for understanding cellular clathrin dynamics.

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