Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca(2+) release channel/ryanodine receptor with calsequestrin.
FEBS Lett
; 472(1): 73-7, 2000 Apr 21.
Article
em En
| MEDLINE
| ID: mdl-10781808
ABSTRACT
A high affinity molecular interaction is demonstrated between calsequestrin and the sarcoplasmic reticular Ca(2+) 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 Ca(2+) 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].
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Retículo Sarcoplasmático
/
Calsequestrina
/
Canal de Liberação de Cálcio do Receptor de Rianodina
Limite:
Animals
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article