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Evidence for a role of C‐terminus in Ca 2+ inactivation of skeletal muscle Ca 2+ release channel (ryanodine receptor)
Author(s) -
Nakai Junichi,
Gao Ling,
Xu Le,
Xin Chunlin,
Pasek Daniel A.,
Meissner Gerhard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01232-6
Subject(s) - ryr1 , ryanodine receptor , ryanodine receptor 2 , chemistry , skeletal muscle , biophysics , receptor , dihydropyridine , biochemistry , calcium , biology , endocrinology , organic chemistry
Six chimeras of the skeletal muscle (RyR1) and cardiac muscle (RyR2) Ca 2+ release channels (ryanodine receptors) previously used to identify RyR1 dihydropyridine receptor interactions [Nakai et al. (1998) J. Biol. Chem. 273, 13403] were expressed in HEK293 cells to assess their Ca 2+ dependence in [ 3 H]ryanodine binding and single channel measurements. The results indicate that the C‐terminal one‐fourth has a major role in Ca 2+ activation and inactivation of RyR1. Further, our results show that replacement of RyR1 regions with corresponding RyR2 regions can result in loss and/or reduction of [ 3 H]ryanodine binding affinity while maintaining channel activity.