Understanding the cooperative interaction between myosin II and actin cross-linkers mediated by actin filaments during mechanosensation.

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 J

journal_title

Biophysical journal

authors

Luo T,Mohan K,Srivastava V,Ren Y,Iglesias PA,Robinson DN

doi

10.1016/j.bpj.2011.12.020

subject

Has Abstract

pub_date

2012-01-18 00:00:00

pages

238-47

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(11)05422-1

journal_volume

102

pub_type

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