Journal
CELL REPORTS
Volume 2, Issue 3, Pages 433-439Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2012.08.014
Keywords
-
Categories
Funding
- European Research Council under the European Union's Seventh Framework Programme (FP7)/ERC SelfOrg [289714]
- Deutsche Forschungsgemeinschaft through the DFG-Cluster of Excellence Nanosystems Initiative Munich
- DFG-SPP [1464]
- European Research Council (ERC) [289714] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
The 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available