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Structural basis for cofilin binding and actin filament disassembly

Author

Listed:
  • Kotaro Tanaka

    (Nagoya University)

  • Shuichi Takeda

    (Nagoya University)

  • Kaoru Mitsuoka

    (Osaka University)

  • Toshiro Oda

    (Tokai Gakuin University)

  • Chieko Kimura-Sakiyama

    (Nagoya University
    Faculty of Life and Medical Sciences)

  • Yuichiro Maéda

    (Nagoya University
    Toyota Physical and Chemical Research Institute)

  • Akihiro Narita

    (Nagoya University)

Abstract

Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin–actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin–actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.

Suggested Citation

  • Kotaro Tanaka & Shuichi Takeda & Kaoru Mitsuoka & Toshiro Oda & Chieko Kimura-Sakiyama & Yuichiro Maéda & Akihiro Narita, 2018. "Structural basis for cofilin binding and actin filament disassembly," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04290-w
    DOI: 10.1038/s41467-018-04290-w
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