The molecular basis of thin filament activation: from single molecule to muscle

Abstract For muscles to effectively power locomotion, trillions of myosin molecules must rapidly attach and detach from the actin thin filament. This is accomplished by precise regulation of the availability of the myosin binding sites on actin (i.e. activation). Both calcium (Ca++) and myosin bindi...

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Autores principales:	Thomas Longyear, Sam Walcott, Edward P. Debold
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/091849787be54845a0c1a0d42faf0dc2
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spelling	oai:doaj.org-article:091849787be54845a0c1a0d42faf0dc22021-12-02T12:32:42ZThe molecular basis of thin filament activation: from single molecule to muscle10.1038/s41598-017-01604-82045-2322https://doaj.org/article/091849787be54845a0c1a0d42faf0dc22017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01604-8https://doaj.org/toc/2045-2322Abstract For muscles to effectively power locomotion, trillions of myosin molecules must rapidly attach and detach from the actin thin filament. This is accomplished by precise regulation of the availability of the myosin binding sites on actin (i.e. activation). Both calcium (Ca++) and myosin binding contribute to activation, but both mechanisms are simultaneously active during contraction, making their relative contributions difficult to determine. Further complicating the process, myosin binding accelerates the attachment rate of neighboring myosin molecules, adding a cooperative element to the activation process. To de-convolve these two effects, we directly determined the effect of Ca++ on the rate of attachment of a single myosin molecule to a single regulated actin thin filament, and separately determined the distance over which myosin binding increases the attachment rate of neighboring molecules. Ca++ alone increases myosin’s attachment rate ~50-fold, while myosin binding accelerates attachment of neighboring molecules 400 nm along the actin thin filament.Thomas LongyearSam WalcottEdward P. DeboldNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Thomas Longyear Sam Walcott Edward P. Debold The molecular basis of thin filament activation: from single molecule to muscle
description	Abstract For muscles to effectively power locomotion, trillions of myosin molecules must rapidly attach and detach from the actin thin filament. This is accomplished by precise regulation of the availability of the myosin binding sites on actin (i.e. activation). Both calcium (Ca++) and myosin binding contribute to activation, but both mechanisms are simultaneously active during contraction, making their relative contributions difficult to determine. Further complicating the process, myosin binding accelerates the attachment rate of neighboring myosin molecules, adding a cooperative element to the activation process. To de-convolve these two effects, we directly determined the effect of Ca++ on the rate of attachment of a single myosin molecule to a single regulated actin thin filament, and separately determined the distance over which myosin binding increases the attachment rate of neighboring molecules. Ca++ alone increases myosin’s attachment rate ~50-fold, while myosin binding accelerates attachment of neighboring molecules 400 nm along the actin thin filament.
format	article
author	Thomas Longyear Sam Walcott Edward P. Debold
author_facet	Thomas Longyear Sam Walcott Edward P. Debold
author_sort	Thomas Longyear
title	The molecular basis of thin filament activation: from single molecule to muscle
title_short	The molecular basis of thin filament activation: from single molecule to muscle
title_full	The molecular basis of thin filament activation: from single molecule to muscle
title_fullStr	The molecular basis of thin filament activation: from single molecule to muscle
title_full_unstemmed	The molecular basis of thin filament activation: from single molecule to muscle
title_sort	molecular basis of thin filament activation: from single molecule to muscle
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/091849787be54845a0c1a0d42faf0dc2
work_keys_str_mv	AT thomaslongyear themolecularbasisofthinfilamentactivationfromsinglemoleculetomuscle AT samwalcott themolecularbasisofthinfilamentactivationfromsinglemoleculetomuscle AT edwardpdebold themolecularbasisofthinfilamentactivationfromsinglemoleculetomuscle AT thomaslongyear molecularbasisofthinfilamentactivationfromsinglemoleculetomuscle AT samwalcott molecularbasisofthinfilamentactivationfromsinglemoleculetomuscle AT edwardpdebold molecularbasisofthinfilamentactivationfromsinglemoleculetomuscle
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The molecular basis of thin filament activation: from single molecule to muscle

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