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

Shashank Shekhar, Johnson Chung, Jane Kondev, Jeff Gelles () and Bruce L. Goode ()
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Shashank Shekhar: Brandeis University
Johnson Chung: Brandeis University
Jane Kondev: Brandeis University
Jeff Gelles: Brandeis University
Bruce L. Goode: Brandeis University

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-13268-1

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