In skeletal muscle, excitation–contraction (E–C) coupling requires the conversion of the depolarization signal of the invaginated surface membrane, namely the transverse (T-) tubule, to Ca2+ release from the sarcoplasmic reticulum (SR). Signal transduction occurs at the junctional complex between the T-tubule and SR, designated as the triad junction, which contains two components essential for E–C coupling, namely the dihydropyridine receptor as the T-tubular voltage sensor and the ryanodine receptor as the SR Ca2+-release channel. However, functional expression of the two receptors seemed to constitute neither the signal-transduction system nor the junction between the surface and intracellular membranes in cultured cells, suggesting that some as-yet-unidentified molecules participate in both the machinery. In addition, the molecular basis of the formation of the triad junction is totally unknown. It is therefore important to examine the components localized to the triad junction. Here we report the identification using monoclonal antibody and primary structure by cDNA cloning of mitsugumin29, a novel transmembrane protein from the triad junction in skeletal muscle. This protein is homologous in amino acid sequence and shares characteristic structural features with the members of the synaptophysin family. The subcellular distribution and protein structure suggest that mitsugumin29 is involved in communication between the T-tubular and junctional SR membranes.
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April 1998
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Research Article|
April 01 1998
Mitsugumin29, a novel synaptophysin family member from the triad junction in skeletal muscle
Hiroshi TAKESHIMA;
Hiroshi TAKESHIMA
1
*Department of Pharmacology, Faculty of Medicine, University of Tokyo, and CREST, Japan Science and Technology Corporation, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan
1To whom correspondence should be addressed.
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Misa SHIMUTA;
Misa SHIMUTA
*Department of Pharmacology, Faculty of Medicine, University of Tokyo, and CREST, Japan Science and Technology Corporation, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan
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Shinji KOMAZAKI;
Shinji KOMAZAKI
†Department of Anatomy, Saitama Medical School, Moroyama-machi, Saitama 350-01, Japan
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Kazuhiro OHMI;
Kazuhiro OHMI
*Department of Pharmacology, Faculty of Medicine, University of Tokyo, and CREST, Japan Science and Technology Corporation, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan
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Miyuki NISHI;
Miyuki NISHI
*Department of Pharmacology, Faculty of Medicine, University of Tokyo, and CREST, Japan Science and Technology Corporation, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan
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Masamitsu IINO;
Masamitsu IINO
*Department of Pharmacology, Faculty of Medicine, University of Tokyo, and CREST, Japan Science and Technology Corporation, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan
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Atsuro MIYATA;
Atsuro MIYATA
‡Department of Biochemistry, National Cardiovascular Center Research Institute, Suita, Osaka 565, Japan
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Kenji KANGAWA
Kenji KANGAWA
‡Department of Biochemistry, National Cardiovascular Center Research Institute, Suita, Osaka 565, Japan
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Publisher: Portland Press Ltd
Received:
October 30 1997
Revision Received:
December 23 1997
Accepted:
January 09 1998
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1998
1998
Biochem J (1998) 331 (1): 317–322.
Article history
Received:
October 30 1997
Revision Received:
December 23 1997
Accepted:
January 09 1998
Citation
Hiroshi TAKESHIMA, Misa SHIMUTA, Shinji KOMAZAKI, Kazuhiro OHMI, Miyuki NISHI, Masamitsu IINO, Atsuro MIYATA, Kenji KANGAWA; Mitsugumin29, a novel synaptophysin family member from the triad junction in skeletal muscle. Biochem J 1 April 1998; 331 (1): 317–322. doi: https://doi.org/10.1042/bj3310317
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