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Skeletal and cardiac ryanodine receptors bind to the Ca 2+ ‐sensor region of dihydropyridine receptor α 1C subunit
Author(s) -
Mouton Jérôme,
Ronjat Michel,
Jona Istvan,
Villaz Michel,
Feltz Anne,
Maulet Yves
Publication year - 2001
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(01)02866-6
Subject(s) - ryanodine receptor , ryr1 , ryanodine receptor 2 , chemistry , biophysics , protein subunit , dihydropyridine , receptor , calcium , calmodulin , voltage dependent calcium channel , skeletal muscle , cardiac muscle , cytoplasm , biochemistry , biology , endocrinology , organic chemistry , gene
In striated muscles, excitation–contraction coupling is mediated by the functional interplay between dihydropyridine receptor L‐type calcium channels (DHPR) and ryanodine receptor calcium‐release channel (RyR). Although significantly different molecular mechanisms are involved in skeletal and cardiac muscles, bidirectional cross‐talk between the two channels has been described in both tissues. In the present study using surface plasmon resonance spectroscopy, we demonstrate that both RyR 1 and RyR 2 can bind to structural elements of the C‐terminal cytoplasmic domain of α 1C . The interaction is restricted to the CB and IQ motifs involved in the calmodulin‐mediated Ca 2+ ‐dependent inactivation of the DHPR, suggesting functional interactions between the two channels.