Biased localization of actin binding proteins by actin filament conformation
Journal Article
·
· Nature Communications
- Univ. of California, Berkeley, CA (United States). Dept. of Bioengineering and Biophysics Program; OSTI
- Univ. of California, Berkeley, CA (United States). Dept. of Bioengineering and Biophysics Program
- Technische Universität München, Garching (Germany). Lehrstuhl für Biophysik (E27)
- Univ. of California, Berkeley, CA (United States). Dept. of Bioengineering and Biophysics Program; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Chan Zuckerberg Biohub, San Francisco, CA (United States)
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.
- Research Organization:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Organization:
- Deutsche Forschungsgemeinschaft (DFG); European Molecular Microbiology Organization (EMBO); Human Frontier Science Program (HFSP); National Institutes of Health (NIH); National Science Foundation (NSF); USDOE Office of Science (SC)
- Grant/Contract Number:
- AC02-05CH11231
- OSTI ID:
- 1815971
- Journal Information:
- Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 11; ISSN 2041-1723
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Similar Records
Steric regulation of tandem calponin homology domain actin-binding affinity
αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
Cortactin Adopts a Globular Conformation and Bundles Actin into Sheets
Journal Article
·
Wed Dec 11 19:00:00 EST 2019
· Molecular Biology of the Cell
·
OSTI ID:1615283
αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
Journal Article
·
Tue Sep 24 20:00:00 EDT 2013
· Molecular Biology of the Cell
·
OSTI ID:1625233
Cortactin Adopts a Globular Conformation and Bundles Actin into Sheets
Journal Article
·
Thu Aug 21 00:00:00 EDT 2008
· J. Biol. Chem.
·
OSTI ID:1006668