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Myosin light chains: Teaching old dogs new tricks
The myosin holoenzyme is a multimeric protein complex consisting of heavy chains and light chains. Myosin light chains are calmodulin family members which are crucially involved in the mechanoenzymatic function of the myosin holoenzyme. This review examines the diversity of light chains within the m...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4914028/ https://www.ncbi.nlm.nih.gov/pubmed/26155737 http://dx.doi.org/10.1080/19490992.2015.1054092 |
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author | Heissler, Sarah M Sellers, James R |
author_facet | Heissler, Sarah M Sellers, James R |
author_sort | Heissler, Sarah M |
collection | PubMed |
description | The myosin holoenzyme is a multimeric protein complex consisting of heavy chains and light chains. Myosin light chains are calmodulin family members which are crucially involved in the mechanoenzymatic function of the myosin holoenzyme. This review examines the diversity of light chains within the myosin superfamily, discusses interactions between the light chain and the myosin heavy chain as well as regulatory and structural functions of the light chain as a subunit of the myosin holoenzyme. It covers aspects of the myosin light chain in the localization of the myosin holoenzyme, protein-protein interactions and light chain binding to non-myosin binding partners. Finally, this review challenges the dogma that myosin regulatory and essential light chain exclusively associate with conventional myosin heavy chains while unconventional myosin heavy chains usually associate with calmodulin. |
format | Online Article Text |
id | pubmed-4914028 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-49140282016-07-11 Myosin light chains: Teaching old dogs new tricks Heissler, Sarah M Sellers, James R Bioarchitecture Review The myosin holoenzyme is a multimeric protein complex consisting of heavy chains and light chains. Myosin light chains are calmodulin family members which are crucially involved in the mechanoenzymatic function of the myosin holoenzyme. This review examines the diversity of light chains within the myosin superfamily, discusses interactions between the light chain and the myosin heavy chain as well as regulatory and structural functions of the light chain as a subunit of the myosin holoenzyme. It covers aspects of the myosin light chain in the localization of the myosin holoenzyme, protein-protein interactions and light chain binding to non-myosin binding partners. Finally, this review challenges the dogma that myosin regulatory and essential light chain exclusively associate with conventional myosin heavy chains while unconventional myosin heavy chains usually associate with calmodulin. Taylor & Francis 2015-07-09 /pmc/articles/PMC4914028/ /pubmed/26155737 http://dx.doi.org/10.1080/19490992.2015.1054092 Text en © 2015 The Author(s). Published by Taylor & Francis http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Heissler, Sarah M Sellers, James R Myosin light chains: Teaching old dogs new tricks |
title | Myosin light chains: Teaching old dogs new tricks |
title_full | Myosin light chains: Teaching old dogs new tricks |
title_fullStr | Myosin light chains: Teaching old dogs new tricks |
title_full_unstemmed | Myosin light chains: Teaching old dogs new tricks |
title_short | Myosin light chains: Teaching old dogs new tricks |
title_sort | myosin light chains: teaching old dogs new tricks |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4914028/ https://www.ncbi.nlm.nih.gov/pubmed/26155737 http://dx.doi.org/10.1080/19490992.2015.1054092 |
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