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Related Experiment Videos

Bound-cation exchange affects the lag phase in actin polymerization.

L C Gershman, J Newman, L A Selden

    Biochemistry
    |May 8, 1984
    PubMed
    Summary

    Actin polymerization

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    Stabilization of cyclic processes by slowly varying forcing.

    Chaos (Woodbury, N.Y.)·2022

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cellular Dynamics

    Background:

    • The lag phase in actin polymerization is typically linked to nucleation.
    • A persistent lag phase exists even when nucleation is bypassed, particularly with Ca2+-actin and MgCl2.

    Purpose of the Study:

    • To investigate the cause of the nucleation-independent lag phase in actin polymerization.
    • To determine the role of divalent cations in actin polymerization kinetics.

    Main Methods:

    • Polymerization assays using phalloidin-stabilized actin nuclei.
    • Treatment of actin with ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) and Mg2+.
    • Measurement of actin-bound cations.

    Main Results:

    • Pretreatment with EGTA and/or Mg2+ significantly reduces or eliminates the lag phase.
    • Direct measurement confirms that Mg2+ replaces Ca2+ bound to actin.
    • This Mg2+-actin species exhibits enhanced polymerizability.

    Conclusions:

    • Divalent cation exchange (Ca2+ to Mg2+) occurs during the nucleation-independent lag phase.
    • This cation exchange is responsible for the persistent lag and is likely the 'monomer activation' step.
    • Understanding cation exchange is crucial for controlling actin polymerization dynamics.

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