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Regulation of actin catch-slip bonds with a RhoA-formin module
- Source :
- Scientific reports, vol 6, iss 1, Scientific Reports, Lee, C-Y; Lou, J; Wen, K-K; McKane, M; Eskin, SG; Rubenstein, PA; et al.(2016). Regulation of actin catch-slip bonds with a RhoA-formin module. SCIENTIFIC REPORTS, 6. doi: 10.1038/srep35058. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/01j7b0m2
- Publication Year :
- 2016
- Publisher :
- Springer Science and Business Media LLC, 2016.
-
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.
- Subjects :
- Models, Molecular
0301 basic medicine
RHOA
1.1 Normal biological development and functioning
Arp2/3 complex
macromolecular substances
Molecular Dynamics Simulation
Article
03 medical and health sciences
Actin remodeling of neurons
Underpinning research
Models
Animals
Actin-binding protein
Binding Sites
Multidisciplinary
biology
Lysine
Microfilament Proteins
Molecular
Actin remodeling
Actin cytoskeleton
Actins
Cell biology
Other Physical Sciences
030104 developmental biology
Amino Acid Substitution
Gene Expression Regulation
Generic Health Relevance
Formins
biology.protein
Biochemistry and Cell Biology
MDia1
rhoA GTP-Binding Protein
Protein Binding
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....b48d5bc1f64f39aae9c0664aba8de132