Journal article
Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic Reticulum
The Journal of biological chemistry, Vol.270(16), pp.9027-9030
04/1995
DOI: 10.1074/jbc.270.16.9027
PMID: 7721813
Abstract
Triadin is a major membrane protein that is specifically localized in the junctional sarcoplasmic reticulum of skeletal muscle and is thought to play an important role in muscle excitation-contraction coupling. In order to identify the proteins in the skeletal muscle that interact with triadin, the cytoplasmic and luminal domains of triadin were expressed as glutathione S-transferase fusion proteins and immobilized to glutathione-Sepharose to form affinity columns. Using these affinity columns, we find that triadin binds specifically to the ryanodine receptor/Ca2+ release channel and the Ca2+ -binding protein calsequestrin from CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid)-solubilized skeletal muscle homogenates. The luminal but not the cytoplasmic domain of triadin-glutathione S-transferase fusion protein binds [3H]ryanodine receptor, whereas neither the cytoplasmic nor the luminal portion of triadin binds [3H]PN-200-100-labeled dihydropyridine receptor. In addition, the luminal domain of triadin interacts with calsequestrin in a Ca2+ -dependent manner and is capable of inhibiting the reassociation of calsequestrin to the junctional face membrane. These results suggest that triadin is the previously unidentified transmembrane protein that anchors calsequestrin to the junctional region of the sarcoplasmic reticulum, and is involved in the functional coupling between calsequestrin and the ryanodine receptor/Ca2+ release channel.
Details
- Title: Subtitle
- Association of Triadin with the Ryanodine Receptor and Calsequestrin in the Lumen of the Sarcoplasmic Reticulum
- Creators
- Wei GuoKevin P Campbell
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.270(16), pp.9027-9030
- DOI
- 10.1074/jbc.270.16.9027
- PMID
- 7721813
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Language
- English
- Date published
- 04/1995
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068272402771
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