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

Anke Herzog, Csaba Szegedi, Istvan Jona, Friedrich W. Herberg, Magdolna Varsanyi

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

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]. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)73-77
Number of pages5
JournalFEBS letters
Volume472
Issue number1
DOIs
Publication statusPublished - Apr 21 2000

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Keywords

  • Ca release
  • Calsequestrin
  • Ryanodine receptor
  • Sarcoplasmic reticulum
  • Striated skeletal muscle
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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