Regulating Contractility of the Actomyosin Cytoskeleton by pH

SummaryThe local interaction of F-actin with myosin-II motor filaments and crosslinking proteins is crucial for the force generation, dynamics, and reorganization of the intracellular cytoskeleton. By using a bottom-up approach, we are able to show that the contractility of reconstituted active actin systems is tightly controlled by the local pH. The pH-dependent intrinsic crossbridge strength of myosin-II is identified to account for a sharp transition of the actin/myosin-II activity from noncontractile to contractile by a change in pH of only 0.1. This pH-dependent contractility is a generic feature, which is observed in all studied crosslinked actin/myosin-II systems. The specific type and concentration of crosslinking protein allows one to sensitively adjust the range of pH where contraction occurs, which can recover the behavior found in Xenopus laevis oocyte extracts. Small variations in pH provide a mechanism of controlling the contractility of cytoskeletal structures, which can be expected to have broad implications in our understanding of cytoskeletal regulation.

Graphical AbstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Contractility of actomyosin systems is tightly regulated by pH ► The pH dependence is tuned by the type and concentration of crosslinking proteins ► The reconstituted system reproduces the pH dependence of mitotic oocyte extracts ► The microscopic origin of the pH-dependent contractility is the network connectivity