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Ryanodine receptors are part of the myospryn complex in cardiac muscle
by
Benson, Matthew A.
, Lai, F. Anthony
, Carlisle, Francesca A.
, Waite, Adrian J.
, George, Christopher H.
, Sweet, Steve M. M.
, Blake, Derek J.
, Ehler, Elisabeth
, Tinsley, Caroline L.
, Martin-Rendon, Enca
in
14
/ 14/19
/ 631/80/304
/ 692/4019/592/75/74
/ 82
/ 82/51
/ 82/58
/ Animals
/ C-Terminus
/ Cardiac muscle
/ Cardiomyocytes
/ Cardiomyopathy
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Chlorocebus aethiops
/ Chromatography, Affinity
/ Chromosome Duplication
/ Chromosomes
/ Cloning, Molecular - methods
/ COS Cells
/ Gene clusters
/ Heart diseases
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Intracellular Signaling Peptides and Proteins
/ Mass Spectrometry
/ Mass spectroscopy
/ Mental disorders
/ Mice
/ multidisciplinary
/ Muscle Proteins - genetics
/ Muscle Proteins - metabolism
/ Receptor density
/ Ryanodine Receptor Calcium Release Channel - metabolism
/ Ryanodine receptors
/ Sarcoplasmic reticulum
/ Sarcoplasmic Reticulum - metabolism
/ Schizophrenia
/ Science
/ Science (multidisciplinary)
/ Skeletal muscle
2017
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Ryanodine receptors are part of the myospryn complex in cardiac muscle
by
Benson, Matthew A.
, Lai, F. Anthony
, Carlisle, Francesca A.
, Waite, Adrian J.
, George, Christopher H.
, Sweet, Steve M. M.
, Blake, Derek J.
, Ehler, Elisabeth
, Tinsley, Caroline L.
, Martin-Rendon, Enca
in
14
/ 14/19
/ 631/80/304
/ 692/4019/592/75/74
/ 82
/ 82/51
/ 82/58
/ Animals
/ C-Terminus
/ Cardiac muscle
/ Cardiomyocytes
/ Cardiomyopathy
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Chlorocebus aethiops
/ Chromatography, Affinity
/ Chromosome Duplication
/ Chromosomes
/ Cloning, Molecular - methods
/ COS Cells
/ Gene clusters
/ Heart diseases
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Intracellular Signaling Peptides and Proteins
/ Mass Spectrometry
/ Mass spectroscopy
/ Mental disorders
/ Mice
/ multidisciplinary
/ Muscle Proteins - genetics
/ Muscle Proteins - metabolism
/ Receptor density
/ Ryanodine Receptor Calcium Release Channel - metabolism
/ Ryanodine receptors
/ Sarcoplasmic reticulum
/ Sarcoplasmic Reticulum - metabolism
/ Schizophrenia
/ Science
/ Science (multidisciplinary)
/ Skeletal muscle
2017
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Ryanodine receptors are part of the myospryn complex in cardiac muscle
by
Benson, Matthew A.
, Lai, F. Anthony
, Carlisle, Francesca A.
, Waite, Adrian J.
, George, Christopher H.
, Sweet, Steve M. M.
, Blake, Derek J.
, Ehler, Elisabeth
, Tinsley, Caroline L.
, Martin-Rendon, Enca
in
14
/ 14/19
/ 631/80/304
/ 692/4019/592/75/74
/ 82
/ 82/51
/ 82/58
/ Animals
/ C-Terminus
/ Cardiac muscle
/ Cardiomyocytes
/ Cardiomyopathy
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Chlorocebus aethiops
/ Chromatography, Affinity
/ Chromosome Duplication
/ Chromosomes
/ Cloning, Molecular - methods
/ COS Cells
/ Gene clusters
/ Heart diseases
/ HEK293 Cells
/ Humanities and Social Sciences
/ Humans
/ Intracellular Signaling Peptides and Proteins
/ Mass Spectrometry
/ Mass spectroscopy
/ Mental disorders
/ Mice
/ multidisciplinary
/ Muscle Proteins - genetics
/ Muscle Proteins - metabolism
/ Receptor density
/ Ryanodine Receptor Calcium Release Channel - metabolism
/ Ryanodine receptors
/ Sarcoplasmic reticulum
/ Sarcoplasmic Reticulum - metabolism
/ Schizophrenia
/ Science
/ Science (multidisciplinary)
/ Skeletal muscle
2017
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Ryanodine receptors are part of the myospryn complex in cardiac muscle
Journal Article
Ryanodine receptors are part of the myospryn complex in cardiac muscle
2017
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Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 82
/ 82/51
/ 82/58
/ Animals
/ Carrier Proteins - metabolism
/ Cloning, Molecular - methods
/ Humanities and Social Sciences
/ Humans
/ Intracellular Signaling Peptides and Proteins
/ Mice
/ Muscle Proteins - metabolism
/ Ryanodine Receptor Calcium Release Channel - metabolism
/ Sarcoplasmic Reticulum - metabolism
/ Science
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