Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca2+ release channel/ryanodine receptor with calsequestrin

FEBS Letters

Jona, Istvan³  Herzog, Anke²  Varsanyi, Magdolna²  Herberg, Friedrich W²  Szegedi, Csaba¹ 

[1] Cell Physiology Research Group of the Hungarian Academy of Science, Debrecen, Hungary;Institut für Physiologische Chemie, Ruhr Universität, D-44780 Bochum, Germany;Department of Physiology, University Medical School, H-4012 Debrecen, Hungary

关键词: Sarcoplasmic reticulum;    Ca2+ release;    Ryanodine receptor;    Calsequestrin;    Striated skeletal muscle;    Surface plasmon resonance;    SR;    sarcoplasmic reticulum;    RyR;    ryanodine receptor;    GST;    glutathione S-transferase;    SPR;    surface plasmon resonance;    RU;    response unit;    aa;    amino acids;    HEPES;    4-(2-hydroxyethyl)-1-piperazine-ethanesulfonic acid;   

DOI  :  10.1016/S0014-5793(00)01431-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A high affinity molecular interaction is demonstrated between calsequestrin and the sarcoplasmic reticular Ca²⁺ release channel/ryanodine receptor (RyR) by surface plasmon resonance. K _D values of 92 nM and 102 nM for the phosphorylated and dephosphorylated calsequestrin have been determined, respectively. Phosphorylation of calsequestrin seems not to influence this high affinity interaction, i.e. calsequestrin might always be bound to RyR. However, the phosphorylation state of calsequestrin determines the amount of Ca²⁺ released from the lumen. Dephosphorylation of approximately 1% of the phosphorylated calsequestrin could be enough to activate the RyR channel half-maximally, as we have shown previously [Szegedi et al., Biochem. J. 337 (1999) 19].

【 授权许可】

Unknown