Biased localization of actin binding proteins by actin filament conformation

Andrew R. Harris, Pamela Jreij, Brian Belardi, Aaron M. Joffe, Andreas R. Bausch and Daniel A. Fletcher ()
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Andrew R. Harris: University of California, Berkeley
Pamela Jreij: University of California, Berkeley
Brian Belardi: University of California, Berkeley
Aaron M. Joffe: University of California, Berkeley
Andreas R. Bausch: Technische Universität München
Daniel A. Fletcher: University of California, Berkeley

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract The assembly of actin filaments into distinct cytoskeletal structures plays a critical role in cell physiology, but how proteins localize differentially to these structures within a shared cytoplasm remains unclear. Here, we show that the actin-binding domains of accessory proteins can be sensitive to filament conformational changes. Using a combination of live cell imaging and in vitro single molecule binding measurements, we show that tandem calponin homology domains (CH1–CH2) can be mutated to preferentially bind actin networks at the front or rear of motile cells. We demonstrate that the binding kinetics of CH1–CH2 domain mutants varies as actin filament conformation is altered by perturbations that include stabilizing drugs and other binding proteins. These findings suggest that conformational changes of actin filaments in cells could help to direct accessory binding proteins to different actin cytoskeletal structures through a biophysical feedback loop.

Date: 2020
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DOI: 10.1038/s41467-020-19768-9

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