Regulation of actin catch-slip bonds with a RhoA-formin module

Cho Yin Lee, Jizhong Lou, Kuo Kuang Wen, Melissa McKane, Suzanne G. Eskin, Peter A. Rubenstein, Shu Chien, Shoichiro Ono, Cheng Zhu, Larry V. McIntire

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13 Scopus citations


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.

Original languageEnglish (US)
Article number35058
JournalScientific reports
StatePublished - Oct 12 2016

All Science Journal Classification (ASJC) codes

  • General


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