Ryanodine receptors are part of the myospryn complex in cardiac muscle

Abstract The Cardiomyopathy–associated gene 5 (Cmya5) encodes myospryn, a large tripartite motif (TRIM)-related protein found predominantly in cardiac and skeletal muscle. Cmya5 is an expression biomarker for a number of diseases affecting striated muscle and may also be a schizophrenia risk gene. T...

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Autores principales:	Matthew A. Benson, Caroline L. Tinsley, Adrian J. Waite, Francesca A. Carlisle, Steve M. M. Sweet, Elisabeth Ehler, Christopher H. George, F. Anthony Lai, Enca Martin-Rendon, Derek J. Blake
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/15612c84e60c4397ba603b292142ca3f
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spelling	oai:doaj.org-article:15612c84e60c4397ba603b292142ca3f2021-12-02T16:07:43ZRyanodine receptors are part of the myospryn complex in cardiac muscle10.1038/s41598-017-06395-62045-2322https://doaj.org/article/15612c84e60c4397ba603b292142ca3f2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06395-6https://doaj.org/toc/2045-2322Abstract The Cardiomyopathy–associated gene 5 (Cmya5) encodes myospryn, a large tripartite motif (TRIM)-related protein found predominantly in cardiac and skeletal muscle. Cmya5 is an expression biomarker for a number of diseases affecting striated muscle and may also be a schizophrenia risk gene. To further understand the function of myospryn in striated muscle, we searched for additional myospryn paralogs. Here we identify a novel muscle-expressed TRIM-related protein minispryn, encoded by Fsd2, that has extensive sequence similarity with the C-terminus of myospryn. Cmya5 and Fsd2 appear to have originated by a chromosomal duplication and are found within evolutionarily-conserved gene clusters on different chromosomes. Using immunoaffinity purification and mass spectrometry we show that minispryn co-purifies with myospryn and the major cardiac ryanodine receptor (RyR2) from heart. Accordingly, myospryn, minispryn and RyR2 co-localise at the junctional sarcoplasmic reticulum of isolated cardiomyocytes. Myospryn redistributes RyR2 into clusters when co-expressed in heterologous cells whereas minispryn lacks this activity. Together these data suggest a novel role for the myospryn complex in the assembly of ryanodine receptor clusters in striated muscle.Matthew A. BensonCaroline L. TinsleyAdrian J. WaiteFrancesca A. CarlisleSteve M. M. SweetElisabeth EhlerChristopher H. GeorgeF. Anthony LaiEnca Martin-RendonDerek J. BlakeNature 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 Matthew A. Benson Caroline L. Tinsley Adrian J. Waite Francesca A. Carlisle Steve M. M. Sweet Elisabeth Ehler Christopher H. George F. Anthony Lai Enca Martin-Rendon Derek J. Blake Ryanodine receptors are part of the myospryn complex in cardiac muscle
description	Abstract The Cardiomyopathy–associated gene 5 (Cmya5) encodes myospryn, a large tripartite motif (TRIM)-related protein found predominantly in cardiac and skeletal muscle. Cmya5 is an expression biomarker for a number of diseases affecting striated muscle and may also be a schizophrenia risk gene. To further understand the function of myospryn in striated muscle, we searched for additional myospryn paralogs. Here we identify a novel muscle-expressed TRIM-related protein minispryn, encoded by Fsd2, that has extensive sequence similarity with the C-terminus of myospryn. Cmya5 and Fsd2 appear to have originated by a chromosomal duplication and are found within evolutionarily-conserved gene clusters on different chromosomes. Using immunoaffinity purification and mass spectrometry we show that minispryn co-purifies with myospryn and the major cardiac ryanodine receptor (RyR2) from heart. Accordingly, myospryn, minispryn and RyR2 co-localise at the junctional sarcoplasmic reticulum of isolated cardiomyocytes. Myospryn redistributes RyR2 into clusters when co-expressed in heterologous cells whereas minispryn lacks this activity. Together these data suggest a novel role for the myospryn complex in the assembly of ryanodine receptor clusters in striated muscle.
format	article
author	Matthew A. Benson Caroline L. Tinsley Adrian J. Waite Francesca A. Carlisle Steve M. M. Sweet Elisabeth Ehler Christopher H. George F. Anthony Lai Enca Martin-Rendon Derek J. Blake
author_facet	Matthew A. Benson Caroline L. Tinsley Adrian J. Waite Francesca A. Carlisle Steve M. M. Sweet Elisabeth Ehler Christopher H. George F. Anthony Lai Enca Martin-Rendon Derek J. Blake
author_sort	Matthew A. Benson
title	Ryanodine receptors are part of the myospryn complex in cardiac muscle
title_short	Ryanodine receptors are part of the myospryn complex in cardiac muscle
title_full	Ryanodine receptors are part of the myospryn complex in cardiac muscle
title_fullStr	Ryanodine receptors are part of the myospryn complex in cardiac muscle
title_full_unstemmed	Ryanodine receptors are part of the myospryn complex in cardiac muscle
title_sort	ryanodine receptors are part of the myospryn complex in cardiac muscle
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/15612c84e60c4397ba603b292142ca3f
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Ryanodine receptors are part of the myospryn complex in cardiac muscle

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