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Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude

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  • Shashank Shekhar

    (Brandeis University
    Brandeis University
    Brandeis University)

  • Johnson Chung

    (Brandeis University)

  • Jane Kondev

    (Brandeis University)

  • Jeff Gelles

    (Brandeis University)

  • Bruce L. Goode

    (Brandeis University)

Abstract

Cellular actin networks can be rapidly disassembled and remodeled in a few seconds, yet in vitro actin filaments depolymerize slowly over minutes. The cellular mechanisms enabling actin to depolymerize this fast have so far remained obscure. Using microfluidics-assisted TIRF, we show that Cyclase-associated protein (CAP) and Cofilin synergize to processively depolymerize actin filament pointed ends at a rate 330-fold faster than spontaneous depolymerization. Single molecule imaging further reveals that hexameric CAP molecules interact with the pointed ends of Cofilin-decorated filaments for several seconds at a time, removing approximately 100 actin subunits per binding event. These findings establish a paradigm, in which a filament end-binding protein and a side-binding protein work in concert to control actin dynamics, and help explain how rapid actin network depolymerization is achieved in cells.

Suggested Citation

  • Shashank Shekhar & Johnson Chung & Jane Kondev & Jeff Gelles & Bruce L. Goode, 2019. "Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13268-1
    DOI: 10.1038/s41467-019-13268-1
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    Cited by:

    1. Micaela Boiero Sanders & Wout Oosterheert & Oliver Hofnagel & Peter Bieling & Stefan Raunser, 2024. "Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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