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Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin

Author

Listed:
  • Tommi Kotila

    (University of Helsinki)

  • Hugo Wioland

    (Institut Jacques Monod)

  • Giray Enkavi

    (University of Helsinki)

  • Konstantin Kogan

    (University of Helsinki)

  • Ilpo Vattulainen

    (University of Helsinki
    Tampere University)

  • Antoine Jégou

    (Institut Jacques Monod)

  • Guillaume Romet-Lemonne

    (Institut Jacques Monod)

  • Pekka Lappalainen

    (University of Helsinki)

Abstract

The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.

Suggested Citation

  • Tommi Kotila & Hugo Wioland & Giray Enkavi & Konstantin Kogan & Ilpo Vattulainen & Antoine Jégou & Guillaume Romet-Lemonne & Pekka Lappalainen, 2019. "Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13213-2
    DOI: 10.1038/s41467-019-13213-2
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    Cited by:

    1. Tommi Kotila & Hugo Wioland & Muniyandi Selvaraj & Konstantin Kogan & Lina Antenucci & Antoine Jégou & Juha T. Huiskonen & Guillaume Romet-Lemonne & Pekka Lappalainen, 2022. "Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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