SRP-27 (sarcoplasmic reticulum protein of 27 kDa) is a newly identified integral membrane protein constituent of the skeletal muscle SR (sarcoplasmic reticulum). We identified its primary structure from cDNA clones isolated from a mouse skeletal muscle cDNA library. ESTs (expressed sequence tags) of SRP-27 were found mainly in cDNA libraries from excitable tissues of mouse. Western blot analysis confirmed the expression of SRP-27 in skeletal muscle and, to a lower extent, in heart and brain. Mild trypsin proteolysis combined with primary-structure prediction analysis suggested that SRP-27 has four transmembrane-spanning alpha helices and its C-terminal domain faces the cytoplasmic side of the endo(sarco)plasmic reticulum. The expression of SRP-27 is higher in fast twitch skeletal muscles compared to slow twitch muscles and peaks during the first month of post-natal development. High-resolution immunohistochemistry and Western blot analysis of subcellular fractions indicated that SRP-27 is distributed in both longitudinal tubules and terminal cisternae of the SR, as well as in the perinuclear membrane systems and the nuclear envelope of myotubes and adult fibres. SRP-27 co-sediments with the RyR (ryanodine receptor) macromolecular complex in high-salt sucrose-gradient centrifugation, and is pulled-down by anti-RyR as well as by maurocalcin, a well characterized RyR modulator. Our results indicate that SRP-27 is part of a SR supramolecular complex, suggesting the involvement of SRP-27 in the structural organization or function of the molecular machinery underlying excitation–contraction coupling.
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April 2008
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Research Article|
March 27 2008
SRP-27 is a novel component of the supramolecular signalling complex involved in skeletal muscle excitation–contraction coupling
Christophe Bleunven;
Christophe Bleunven
*Department of Experimental and Diagnostic Medicine, General Pathology section, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy
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Susan Treves;
Susan Treves
*Department of Experimental and Diagnostic Medicine, General Pathology section, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy
†Department of Anesthesia, ZLF Basel University Hospital, Basel, Hebelstrasse 20, 4031 Basel, Switzerland
‡Department of Research, ZLF Basel University Hospital, Basel, Hebelstrasse 20, 4031 Basel, Switzerland
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Xia Jinyu;
Xia Jinyu
*Department of Experimental and Diagnostic Medicine, General Pathology section, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy
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Elisa Leo;
Elisa Leo
*Department of Experimental and Diagnostic Medicine, General Pathology section, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy
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Michel Ronjat;
Michel Ronjat
§Laboratoire Canaux Calciques, iRTSV/CCFP CEA Grenoble INSERM U836 Institut des Neurosciences Grenoble GIN, 17 rue des Martyrs, 38054 Grenoble Cedex 09, France
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Michel De Waard;
Michel De Waard
§Laboratoire Canaux Calciques, iRTSV/CCFP CEA Grenoble INSERM U836 Institut des Neurosciences Grenoble GIN, 17 rue des Martyrs, 38054 Grenoble Cedex 09, France
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Georg Kern;
Georg Kern
∥Department of Physiology and Medical Physics, Medical University Innsbruck, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria
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Francesco Zorzato
Francesco Zorzato
1
*Department of Experimental and Diagnostic Medicine, General Pathology section, University of Ferrara, Via Borsari 46, 44100 Ferrara, Italy
†Department of Anesthesia, ZLF Basel University Hospital, Basel, Hebelstrasse 20, 4031 Basel, Switzerland
1To whom correspondence should be addressed (email zor@unife.it).
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Biochem J (2008) 411 (2): 343–349.
Article history
Received:
July 10 2007
Revision Received:
November 23 2007
Accepted:
November 26 2007
Accepted Manuscript online:
November 26 2007
Citation
Christophe Bleunven, Susan Treves, Xia Jinyu, Elisa Leo, Michel Ronjat, Michel De Waard, Georg Kern, Bernhard E. Flucher, Francesco Zorzato; SRP-27 is a novel component of the supramolecular signalling complex involved in skeletal muscle excitation–contraction coupling. Biochem J 15 April 2008; 411 (2): 343–349. doi: https://doi.org/10.1042/BJ20070906
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