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CASQ2 can be phosphorylated by three different kinases: casein kinase I (CK I), casein kinase II (CK II) and ε protein kinase C1 (εPKC1).<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> CK II is located in the SR and is able to phosphorylate Ser 378, Ser 382 and Ser 386. These residues are on the C-terminal domain.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> The consensus sequence recognized by CK II is Ser/Thr-X-X-Asp/Glu.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> The phosphorylation is more likely if there are acidic residues after this consensus sequence.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref>
CASQ2 can be phosphorylated by three different kinases: casein kinase I (CK I), casein kinase II (CK II) and ε protein kinase C1 (εPKC1).<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> CK II is located in the SR and is able to phosphorylate Ser 378, Ser 382 and Ser 386. These residues are on the C-terminal domain.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> The consensus sequence recognized by CK II is Ser/Thr-X-X-Asp/Glu.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> The phosphorylation is more likely if there are acidic residues after this consensus sequence.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref>


The phosphorylation and de-phosphorylation of CASQ2 may provide an off/on switch for CASQ2 to regulate Ca<sup>2+</sup> capture. But there is not any proof yet.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> However it is known that phosphorylations on CASQ2 modify the interactions between CASQ2 and RyR but not between CASQ2 and Triadin and Junctin.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref>
The phosphorylation and dephosphorylation of CASQ2 may provide an off/on switch for CASQ2 to regulate Ca<sup>2+</sup> capture. But there is not any proof yet.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref> However it is known that phosphorylations on CASQ2 modify the interactions between CASQ2 and RyR but not between CASQ2 and Triadin and Junctin.<ref name="Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004)">http://www.ncbi.nlm.nih.gov/pubmed/15050380</ref>




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OCA, Marc-Antoine Jaques, Thomas Vuillemin, Stéphanie Gross