Abstract:
: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 cooperative interactions between bound myosin heads. By assuming that the binding of myosin heads induces and/or stabilizes local conformational changes in the actin filaments that enhances myosin II binding locally, we successfully simulate the cooperative binding of myosin to actin observed experimentally. In addition, we can interpret the cooperative interactions between myosin and actin cross-linking proteins 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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Luo T,Mohan K,Srivastava V,Ren Y,Iglesias PA,Robinson DNdoi
10.1016/j.bpj.2011.12.020subject
Has Abstractpub_date
2012-01-18 00:00:00pages
238-47issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(11)05422-1journal_volume
102pub_type
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