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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Harris AR,Jreij P,Belardi B,Joffe AM,Bausch AR,Fletcher DAdoi
10.1038/s41467-020-19768-9subject
Has Abstractpub_date
2020-11-25 00:00:00pages
5973issue
1issn
2041-1723pii
10.1038/s41467-020-19768-9journal_volume
11pub_type
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