Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction

We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са(2+) concentrations and the Са(2+)-sensitivity of the actin-myosin inter...

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Autores principales: Shchepkin, D.V., Matyushenko, A. M., Kopylova, G. V., Artemova, N. V., Bershitsky, S. Y., Tsaturyan, A. K., Levitsky, D. I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2013
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3848074/
https://www.ncbi.nlm.nih.gov/pubmed/24303208
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author Shchepkin, D.V.
Matyushenko, A. M.
Kopylova, G. V.
Artemova, N. V.
Bershitsky, S. Y.
Tsaturyan, A. K.
Levitsky, D. I.
author_facet Shchepkin, D.V.
Matyushenko, A. M.
Kopylova, G. V.
Artemova, N. V.
Bershitsky, S. Y.
Tsaturyan, A. K.
Levitsky, D. I.
author_sort Shchepkin, D.V.
collection PubMed
description We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са(2+) concentrations and the Са(2+)-sensitivity of the actin-myosin interaction underlying this sliding. Based on an analysis of the recently published data on the structure of the actin–Tm–myosin complex, we suppose that the physiological effects of these mutations in Tm can be accounted for by their influence on the interactions between the central part of Tm and certain sites of the myosin head.
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spelling pubmed-38480742013-12-03 Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction Shchepkin, D.V. Matyushenko, A. M. Kopylova, G. V. Artemova, N. V. Bershitsky, S. Y. Tsaturyan, A. K. Levitsky, D. I. Acta Naturae Research Article We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са(2+) concentrations and the Са(2+)-sensitivity of the actin-myosin interaction underlying this sliding. Based on an analysis of the recently published data on the structure of the actin–Tm–myosin complex, we suppose that the physiological effects of these mutations in Tm can be accounted for by their influence on the interactions between the central part of Tm and certain sites of the myosin head. A.I. Gordeyev 2013 /pmc/articles/PMC3848074/ /pubmed/24303208 Text en Copyright © 2013 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Shchepkin, D.V.
Matyushenko, A. M.
Kopylova, G. V.
Artemova, N. V.
Bershitsky, S. Y.
Tsaturyan, A. K.
Levitsky, D. I.
Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title_full Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title_fullStr Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title_full_unstemmed Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title_short Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction
title_sort stabilization of the central part of tropomyosin molecule alters the ca2+-sensitivity of actin-myosin interaction
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3848074/
https://www.ncbi.nlm.nih.gov/pubmed/24303208
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