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Clathrin light chains are calcium-binding proteins.

M J Mooibroek, D F Michiel, J H Wang

    The Journal of Biological Chemistry
    |January 5, 1987
    PubMed
    Summary
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    Clathrin light chains were investigated and found to be calcium-binding proteins. These proteins bind calcium ions, a function that persists even when they are part of larger clathrin structures.

    Area of Science:

    • Biochemistry
    • Cell Biology

    Background:

    • Clathrin is a protein complex essential for vesicle formation.
    • Clathrin light chains (CLCs) have unknown functions.
    • Silver staining can obscure low-abundance proteins like CLCs.

    Purpose of the Study:

    • To investigate the biochemical properties of purified clathrin light chains.
    • To determine if clathrin light chains possess calcium-binding capabilities.

    Main Methods:

    • Purification of clathrin light chains.
    • Sodium dodecyl sulfate gel electrophoresis with silver staining.
    • 45Ca2+ binding assays using nitrocellulose filters.
    • Gel filtration chromatography.
    • Equilibrium dialysis.

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    Main Results:

    • Purified clathrin light chains were not detected by silver staining, suggesting low abundance or unusual properties.
    • Clathrin light chains demonstrated specific binding of 45Ca2+ in the presence of magnesium ions.
    • Binding studies revealed that clathrin light chains bind 1 mole of Ca2+ per mole of light chain with a dissociation constant (Kd) of 25-55 µM.
    • Calcium-binding capacity was retained when light chains were part of triskelion structures, with a Kd of approximately 45 µM.

    Conclusions:

    • Clathrin light chains are identified as calcium-binding proteins.
    • This calcium-binding function is intrinsic to the light chains and is maintained within the clathrin complex.