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Nonlinear Actomyosin Elasticity in Muscle?
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.ORCID iD: 0000-0002-5889-7792
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. McGill Univ, Canada;Karolinska Institutet.ORCID iD: 0000-0003-2819-3046
McGill Univ, Canada.
McGill Univ, Canada.
2019 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 116, no 2, p. 330-346Article in journal (Refereed) Published
Abstract [en]

Cyclic interactions between myosin II motor domains and actin filaments that are powered by turnover of ATP underlie muscle contraction and have key roles in motility of nonmuscle cells. The elastic characteristics of actin-myosin cross-bridges are central in the force-generating process, and disturbances in these properties may lead to disease. Although the prevailing paradigm is that the cross-bridge elasticity is linear (Hookean), recent single-molecule studies suggest otherwise. Despite convincing evidence for substantial nonlinearity of the cross-bridge elasticity in the single-molecule work, this finding has had limited influence on muscle physiology and physiology of other ordered cellular actin-myosin ensembles. Here, we use a biophysical modeling approach to close the gap between single molecules and physiology. The model is used for analysis of available experimental results in the light of possible nonlinearity of the cross-bridge elasticity. We consider results obtained both under rigor conditions (in the absence of ATP) and during active muscle contraction. Our results suggest that a wide range of experimental findings from mechanical experiments on muscle cells are consistent with nonlinear actin-myosin elasticity similar to that previously found in single molecules. Indeed, the introduction of nonlinear cross-bridge elasticity into the model improves the reproduction of key experimental results and eliminates the need for force dependence of the ATP-induced detachment rate, consistent with observations in other single-molecule studies. The findings have significant implications for the understanding of key features of actin-myosin-based production of force and motion in living cells, particularly in muscle, and for the interpretation of experimental results that rely on stiffness measurements on cells or myofibrils.

Place, publisher, year, edition, pages
Cell Press , 2019. Vol. 116, no 2, p. 330-346
National Category
Biophysics
Research subject
Chemistry, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-80278DOI: 10.1016/j.bpj.2018.12.004ISI: 000456327100015PubMedID: 30606448Scopus ID: 2-s2.0-85059232890OAI: oai:DiVA.org:lnu-80278DiVA, id: diva2:1286609
Available from: 2019-02-07 Created: 2019-02-07 Last updated: 2019-08-29Bibliographically approved

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Månsson, AlfPersson, Malin

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