Skeletal and cardiac ryanodine receptors bind to the Ca2+‐sensor region of dihydropyridine receptor α1C subunit

FEBS Letters

Feltz, Anne¹  Jona, Istvan²  Mouton, Jérôme¹  Ronjat, Michel³  Maulet, Yves¹  Villaz, Michel³ 

[1] Laboratoire de Neurobiologie Cellulaire, CNRS FRE 2180, 5 rue Blaise Pascal, 67084 Strasbourg, France;Department of Physiology, University Medical School Debrecen, P.O. Box 22, H-4012 Debrecen, Hungary;Laboratoire Canaux Ioniques et Signalisation, E-9931 INSERM, DBMS, 17 rue des Martyrs, 38054 Grenoble, France

关键词: Calcium channel;    Dihydropyridine receptor;    Ryanodine receptor;    Excitation–contraction coupling;    DHPR;    dihydropyridine receptor L-type calcium channel;    RyR;    ryanodine receptor calcium-release channel;    InsP3;    inositol triphosphate;    EC;    excitation–contraction;    DCCR;    directly coupled calcium release;    CICR;    calcium-induced calcium release;    SPR;    surface plasmon resonance spectroscopy;    RU;    resonance units;    VSRM;    voltage-sensitive release mechanism;   

DOI  :  10.1016/S0014-5793(01)02866-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 RyR₁ and RyR₂ 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 Ca²⁺-dependent inactivation of the DHPR, suggesting functional interactions between the two channels.

【 授权许可】

Unknown