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Kinetics of actin elongation and depolymerization at the pointed end.

A Weber, J Northrop, M F Bishop

    Biochemistry
    |May 5, 1987
    PubMed
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    Villin-capped actin filaments exhibit nonlinear elongation rates dependent on G-actin concentration. Smaller nuclei (VA3) showed exaggerated nonlinearity, elongating below critical concentrations due to villin-actin complexes.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Biophysics

    Background:

    • Actin dynamics are crucial for cellular processes.
    • Villin caps actin filaments, influencing polymerization.
    • Understanding G-actin concentration effects on filament elongation is key.

    Purpose of the Study:

    • To measure the G-actin concentration-dependent elongation rate (J(c) function) at the pointed end of villin-capped actin filaments.
    • To investigate the influence of nucleus size (VA3 and VA18) on this J(c) function.
    • To explore the role of villin-actin complexes in filament elongation.

    Main Methods:

    • Elongation rate measurements of villin-capped actin filaments at the pointed end.
    • Utilized small (VA3) and large (VA18) actin/villin nuclei.

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  • Performed experiments under physiological conditions with Mg2+ and K+.

    • Main Results:

    • The J(c) function for pointed end elongation was nonlinear for both VA3 and VA18.
    • Lowering monomer concentration near or below the critical concentration (c infinity) caused a sharp decrease in the J(c) function slope.
    • VA3 showed exaggerated nonlinearity, elongating below the critical concentration, suggesting villin-actin complex involvement.

    Conclusions:

    • Villin capping leads to nonlinear G-actin concentration-dependent elongation at the pointed filament end.
    • Nucleus size significantly impacts the nonlinearity of the J(c) function.
    • Free villin and villin-actin oligomers influence elongation rates, with oligomers exhibiting higher actin binding rates.