Latrunculin A Depolymerizes Actin Filaments by Binding Terminal Subunits and by Sequestering Actin Monomers

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  • FUJIWARA Ikuko
    Research Administration Office, Nagoya Institute of Technology Present Address: Graduate School of Science, Osaka City University

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Other Title
  • ラトランキュリンAはアクチンモノマーだけでなくアクチン線維にも結合して脱重合を促進する
  • ラトランキュリン A ワ アクチンモノマー ダケ デ ナク アクチン センイ ニ モ ケツゴウ シテ ダツジュウゴウ オ ソクシン スル

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<p>Latrunculin A (LatA) is the widely used reagent to depolymerize actin filaments. Its mechanism has been thought that LatA sequesters actin monomers from polymerization. Recent observation of single actin filaments by TIRF microscopy found that the binding affinity of LatA to actin monomers depends on the nucleotide status on actin. The observation of actin filaments also showed that LatA binds to actin filaments. LatA increased the depolymerization rate at ends of filaments assembled from ATP-actin to the rates of ADP-actin, but did not change these rates of ADP- or ADP-Pi-bound actin filaments. LatA also severed actin filaments. Thermodynamic analysis proposes that LatA accelerates phosphate release only at ends of actin filaments. Rapid depolymerization, severing and sequestering monomers are mechanisms of LatA to inhibit cellular actin cytoskeleton.</p>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 59 (4), 192-196, 2019

    The Biophysical Society of Japan General Incorporated Association

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