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Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders
Calsequestrin is among the most abundant proteins in muscle sarcoplasmic reticulum and displays a high capacity but a low affinity for Ca(2+) binding. In mammals, calsequestrin is encoded by two genes, CASQ1 and CASQ2, which are expressed almost exclusively in skeletal and cardiac muscles, respectiv...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7582152/ https://www.ncbi.nlm.nih.gov/pubmed/33093545 http://dx.doi.org/10.1038/s41598-020-75097-3 |
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author | Wang, Qian Paskevicius, Tautvydas Filbert, Alexander Qin, Wenying Kim, Hyeong Jin Chen, Xing-Zhen Tang, Jingfeng Dacks, Joel B. Agellon, Luis B. Michalak, Marek |
author_facet | Wang, Qian Paskevicius, Tautvydas Filbert, Alexander Qin, Wenying Kim, Hyeong Jin Chen, Xing-Zhen Tang, Jingfeng Dacks, Joel B. Agellon, Luis B. Michalak, Marek |
author_sort | Wang, Qian |
collection | PubMed |
description | Calsequestrin is among the most abundant proteins in muscle sarcoplasmic reticulum and displays a high capacity but a low affinity for Ca(2+) binding. In mammals, calsequestrin is encoded by two genes, CASQ1 and CASQ2, which are expressed almost exclusively in skeletal and cardiac muscles, respectively. Phylogenetic analysis indicates that calsequestrin is an ancient gene in metazoans, and that the duplication of the ancestral calsequestrin gene took place after the emergence of the lancelet. CASQ2 gene variants associated with catecholaminergic polymorphic ventricular tachycardia (CPVT) in humans are positively correlated with a high degree of evolutionary conservation across all calsequestrin homologues. The mutations are distributed in diverse locations of the calsequestrin protein and impart functional diversity but remarkably manifest in a similar phenotype in humans. |
format | Online Article Text |
id | pubmed-7582152 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-75821522020-10-23 Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders Wang, Qian Paskevicius, Tautvydas Filbert, Alexander Qin, Wenying Kim, Hyeong Jin Chen, Xing-Zhen Tang, Jingfeng Dacks, Joel B. Agellon, Luis B. Michalak, Marek Sci Rep Article Calsequestrin is among the most abundant proteins in muscle sarcoplasmic reticulum and displays a high capacity but a low affinity for Ca(2+) binding. In mammals, calsequestrin is encoded by two genes, CASQ1 and CASQ2, which are expressed almost exclusively in skeletal and cardiac muscles, respectively. Phylogenetic analysis indicates that calsequestrin is an ancient gene in metazoans, and that the duplication of the ancestral calsequestrin gene took place after the emergence of the lancelet. CASQ2 gene variants associated with catecholaminergic polymorphic ventricular tachycardia (CPVT) in humans are positively correlated with a high degree of evolutionary conservation across all calsequestrin homologues. The mutations are distributed in diverse locations of the calsequestrin protein and impart functional diversity but remarkably manifest in a similar phenotype in humans. Nature Publishing Group UK 2020-10-22 /pmc/articles/PMC7582152/ /pubmed/33093545 http://dx.doi.org/10.1038/s41598-020-75097-3 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Wang, Qian Paskevicius, Tautvydas Filbert, Alexander Qin, Wenying Kim, Hyeong Jin Chen, Xing-Zhen Tang, Jingfeng Dacks, Joel B. Agellon, Luis B. Michalak, Marek Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title | Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title_full | Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title_fullStr | Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title_full_unstemmed | Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title_short | Phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
title_sort | phylogenetic and biochemical analysis of calsequestrin structure and association of its variants with cardiac disorders |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7582152/ https://www.ncbi.nlm.nih.gov/pubmed/33093545 http://dx.doi.org/10.1038/s41598-020-75097-3 |
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