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Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle

Myosin-Binding protein-C (MyBP-C) is a family of accessory proteins of striated muscles that contributes to the assembly and stabilization of thick filaments, and regulates the formation of actomyosin cross-bridges, via direct interactions with both thick myosin and thin actin filaments. Three disti...

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Detalles Bibliográficos
Autores principales: Ackermann, Maegen A., Kontrogianni-Konstantopoulos, Aikaterini
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3196898/
https://www.ncbi.nlm.nih.gov/pubmed/22028592
http://dx.doi.org/10.1155/2011/636403
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author Ackermann, Maegen A.
Kontrogianni-Konstantopoulos, Aikaterini
author_facet Ackermann, Maegen A.
Kontrogianni-Konstantopoulos, Aikaterini
author_sort Ackermann, Maegen A.
collection PubMed
description Myosin-Binding protein-C (MyBP-C) is a family of accessory proteins of striated muscles that contributes to the assembly and stabilization of thick filaments, and regulates the formation of actomyosin cross-bridges, via direct interactions with both thick myosin and thin actin filaments. Three distinct MyBP-C isoforms have been characterized; cardiac, slow skeletal, and fast skeletal. Numerous mutations in the gene for cardiac MyBP-C (cMyBP-C) have been associated with familial hypertrophic cardiomyopathy (FHC) and have led to increased interest in the regulation and roles of the cardiac isoform. This review will summarize our current knowledge on MyBP-C and its role in modulating contractility, focusing on its interactions with both myosin and actin filaments in cardiac and skeletal muscles.
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spelling pubmed-31968982011-10-25 Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle Ackermann, Maegen A. Kontrogianni-Konstantopoulos, Aikaterini J Biomed Biotechnol Review Article Myosin-Binding protein-C (MyBP-C) is a family of accessory proteins of striated muscles that contributes to the assembly and stabilization of thick filaments, and regulates the formation of actomyosin cross-bridges, via direct interactions with both thick myosin and thin actin filaments. Three distinct MyBP-C isoforms have been characterized; cardiac, slow skeletal, and fast skeletal. Numerous mutations in the gene for cardiac MyBP-C (cMyBP-C) have been associated with familial hypertrophic cardiomyopathy (FHC) and have led to increased interest in the regulation and roles of the cardiac isoform. This review will summarize our current knowledge on MyBP-C and its role in modulating contractility, focusing on its interactions with both myosin and actin filaments in cardiac and skeletal muscles. Hindawi Publishing Corporation 2011 2011-10-16 /pmc/articles/PMC3196898/ /pubmed/22028592 http://dx.doi.org/10.1155/2011/636403 Text en Copyright © 2011 M. A. Ackermann and A. Kontrogianni-Konstantopoulos. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Ackermann, Maegen A.
Kontrogianni-Konstantopoulos, Aikaterini
Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title_full Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title_fullStr Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title_full_unstemmed Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title_short Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle
title_sort myosin binding protein-c: a regulator of actomyosin interaction in striated muscle
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3196898/
https://www.ncbi.nlm.nih.gov/pubmed/22028592
http://dx.doi.org/10.1155/2011/636403
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