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Calcium dependence of villin-induced actin depolymerization.

T P Walsh, A Weber, K Davis

    Biochemistry
    |December 4, 1984
    PubMed
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    Villin protein "cuts" actin filaments at high calcium levels, distinct from its "capping" action at low calcium. This cutting activity suggests different calcium-binding sites regulate these distinct villin functions.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Biophysics

    Background:

    • Actin filaments are crucial for cell structure and motility.
    • Villin is a protein that interacts with actin filaments.
    • Calcium ions are known to regulate various cellular processes, including protein-actin interactions.

    Purpose of the Study:

    • To investigate the mechanism by which villin affects actin filament depolymerization.
    • To determine the role of calcium concentration in mediating villin's interaction with actin.
    • To differentiate between villin's actin-capping and actin-cutting activities.

    Main Methods:

    • Time-course analysis of actin filament depolymerization.
    • Use of fluorescently labeled actin filaments.
    • Experimentation with varying concentrations of calcium, villin, potassium, and magnesium.

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    Main Results:

    • At low calcium, villin inhibits depolymerization by capping filament ends.
    • At high calcium (200 microM), villin accelerates depolymerization, indicating filament cutting.
    • The depolymerization rate at high calcium exceeds that of controls without villin.

    Conclusions:

    • Villin exhibits distinct functions on actin filaments dependent on calcium concentration: capping at low calcium and cutting at high calcium.
    • Different calcium-binding sites on villin likely regulate capping and cutting.
    • The calcium-binding sites for cutting have a lower affinity for calcium than those for capping.