Journal article
Regulation of actin catch-slip bonds with a RhoA-formin module
Scientific reports, Vol.6(1), pp.35058-35058
10/12/2016
DOI: 10.1038/srep35058
PMCID: PMC5059732
PMID: 27731359
Abstract
The dynamic turnover of the actin cytoskeleton is regulated cooperatively by force and biochemical signaling. We previously demonstrated that actin depolymerization under force is governed by catch-slip bonds mediated by force-induced K113:E195 salt-bridges. Yet, the biochemical regulation as well as the functional significance of actin catch bonds has not been elucidated. Using AFM force-clamp experiments, we show that formin controlled by RhoA switches the actin catch-slip bonds to slip-only bonds. SMD simulations reveal that the force does not induce the K113:E195 interaction when formin binds to actin K118 and E117 residues located at the helical segment extending to K113. Actin catch-slip bonds are suppressed by single residue replacements K113E and E195K that interrupt the force-induced K113:E195 interaction; and this suppression is rescued by a K113E/E195K double mutant (E/K) restoring the interaction in the opposite orientation. These results support the biological significance of actin catch bonds, as they corroborate reported observations that RhoA and formin switch force-induced actin cytoskeleton alignment and that either K113E or E195K induces yeast cell growth defects rescued by E/K. Our study demonstrates how the mechano-regulation of actin dynamics is modulated by biochemical signaling molecules, and suggests that actin catch bonds may be important in cell functions.
Details
- Title: Subtitle
- Regulation of actin catch-slip bonds with a RhoA-formin module
- Creators
- Cho-Yin Lee - Division of Radiation Oncology, Department of Oncology, National Taiwan University Hospital and National Taiwan University Cancer Center, Taipei, TaiwanJizhong Lou - Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaKuo-Kuang Wen - Department of Biochemistry, University of Iowa, Iowa City, IA, USAMelissa McKane - Department of Biochemistry, University of Iowa, Iowa City, IA, USASuzanne G Eskin - Institute for Bioengineering and Biosciences, Georgia Institute of Technology and Emory University, Atlanta, GA, USAPeter A Rubenstein - Department of Biochemistry, University of Iowa, Iowa City, IA, USAShu Chien - Department of Bioengineering and Institute of Engineering in Medicine, University of California at San Diego, La Jolla, CA, USAShoichiro Ono - Department of Pathology, Emory University, Atlanta, GA, USACheng Zhu - Institute for Bioengineering and Biosciences, Georgia Institute of Technology and Emory University, Atlanta, GA, USALarry V McIntire - Institute for Bioengineering and Biosciences, Georgia Institute of Technology and Emory University, Atlanta, GA, USA
- Resource Type
- Journal article
- Publication Details
- Scientific reports, Vol.6(1), pp.35058-35058
- DOI
- 10.1038/srep35058
- PMID
- 27731359
- PMCID
- PMC5059732
- NLM abbreviation
- Sci Rep
- ISSN
- 2045-2322
- eISSN
- 2045-2322
- Publisher
- England
- Grant note
- R01 GM033689 / NIGMS NIH HHS R01 HL018672 / NHLBI NIH HHS R01 HL132019 / NHLBI NIH HHS R37 HL018672 / NHLBI NIH HHS R01 HL070537 / NHLBI NIH HHS R01 AI044902 / NIAID NIH HHS R01 AR048615 / NIAMS NIH HHS R21 AI044902 / NIAID NIH HHS
- Language
- English
- Date published
- 10/12/2016
- Academic Unit
- Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
- Record Identifier
- 9984024505602771
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