Sandbox Reserved 820: Difference between revisions
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== Interaction between CASQ2 and <!-- (plutôt Triadin et Junctin) -->RYR == | == Interaction between CASQ2 and <!-- (plutôt Triadin et Junctin) -->RYR == | ||
=== Binding sites === | |||
CASQ2 is anchored into the membrane of SR thanks to two integral proteins: the triadin and the junctin. Triadin as well as Juctin can bind to CASQ2 because of its KEKE motif between the amino acids 210 and 224 for the triadin. The binding site of CASQ2 for the both protein is the Asp-rich region of the C-terminal region. | CASQ2 is anchored into the membrane of SR thanks to two integral proteins: the triadin and the junctin. Triadin as well as Juctin can bind to CASQ2 because of its KEKE motif between the amino acids 210 and 224 for the triadin. The binding site of CASQ2 for the both protein is the Asp-rich region of the C-terminal region. | ||
Triadin and Junctin interact with Ryanodin Receptor (RyR). | Triadin and Junctin interact with Ryanodin Receptor (RyR). | ||
The binding site of CASQ2 to RyR is unknow. | |||
=== Consequences of the bound of CASQ2 === | |||
When CASQ2 binds to Triadin and Junctin, it induces the inhibition of RyR and when CASQ2 unbinds Triadin and Junctin , it induces the activation of Ryr and an efflux of Ca2+ from the SR to the cytoplasm. CASQ2 is free when the concentration of Ca2+ is higher than 1 mM in the SR lumen. | |||
<!-- Source: Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004) Lien: http://www.ncbi.nlm.nih.gov/pubmed/15050380 --> | |||
<!-- Source: Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005) Lien: http://www.ncbi.nlm.nih.gov/pubmed/15731387 --> | |||
== Regulation of CASQ2 == | == Regulation of CASQ2 == | ||
