Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain

J Cell Sci. 2016 Nov 1;129(21):3983-3988. doi: 10.1242/jcs.191643. Epub 2016 Sep 8.

Abstract

Cardiac muscle contraction requires sarcoplasmic reticulum (SR) Ca2+ release mediated by the quaternary complex comprising the ryanodine receptor 2 (RyR2), calsequestrin 2 (CSQ2), junctin (encoded by ASPH) and triadin. Here, we demonstrate that a direct interaction exists between RyR2 and CSQ2. Topologically, CSQ2 binding occurs at the first luminal loop of RyR2. Co-expression of RyR2 and CSQ2 in a human cell line devoid of the other quaternary complex proteins results in altered Ca2+-release dynamics compared to cells expressing RyR2 only. These findings provide a new perspective for understanding the SR luminal Ca2+ sensor and its involvement in cardiac physiology and disease.

Keywords: Ca2+ intracellular release; Calsequestrin; Excitation-contraction coupling; Luminal Ca2+ sensor; Protein–protein interaction; Ryanodine receptor; Sarcoplasmic reticulum.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium / metabolism
  • Calsequestrin / metabolism*
  • HEK293 Cells
  • Humans
  • Intracellular Space / metabolism
  • Myocardium / metabolism*
  • Protein Binding
  • Protein Domains
  • Protein Interaction Mapping
  • Protein Structure, Secondary
  • Ryanodine Receptor Calcium Release Channel / chemistry
  • Ryanodine Receptor Calcium Release Channel / metabolism*

Substances

  • Calsequestrin
  • Ryanodine Receptor Calcium Release Channel
  • Calcium