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Understanding the Cooperative Interaction between Myosin II and Actin Crosslinkers Mediated by Actin Filaments

Tian Zhi Luo's picture

Myosin II is a central mechanoenzyme in a wide range of cellular morphogenic processes. Its cellular localization is dependent not only on signal transduction pathways, but also on mechanical stress. We suggest that this stress-dependent distribution is the result of both the force-dependent binding to actin filaments and cooperativie interactions between bound myosin heads. By assuming that the binding of myosin heads induces and/or stabilizes local conformational changes in the actin filaments which enhances myosin II binding locally, we successfullly simulate the cooperative binding of myosin to actin observed experimentally. In addition, we can interpret the cooperative interactions between myosin and actin-crosslinking protein observed in cellular mechanosensation, provided that a similar mechanism operates among different proteins. Finally, we present a model that couples cooperative interactions to the assembly dynamics of myosin bipolar thick filaments and that accounts for the transient behaviors of the myosin II accumulation during mechanosensation. This mechanism is likely to  be general for a range of myosin II-dependent cellular mechanosensory processes.

 

The attachement includes the manuscript and 3 gif files obstained from simulations (use "windows picture and fax viewer" or other gif players to view the gif files).

 

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