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<!-- Source ASP-rich: The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+‡ and interacts with triadin (Shin et al., 2000) Lien: http://www.sciencedirect.com/science/article/pii/S0014579300022468 -->
<!-- Source ASP-rich: The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca2+‡ and interacts with triadin (Shin et al., 2000) Lien: http://www.sciencedirect.com/science/article/pii/S0014579300022468 -->


== Interaction between CASQ2 and <!-- (plutôt Triadin et Junctin) -->RYR ==
== Interaction between CASQ2, Junctin and Triadin  ==


=== Binding sites ===   
=== Binding sites ===   
CASQ2 is anchored into the membrane of SR thanks to two integral proteins: the triadin and the junctin.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">PMID:15731387</ref> Triadin as well as Juctin can bind to CASQ2 because of its KEKE motif between the amino acids 210 and 224 for the triadin.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref> The binding site of CASQ2 for the both protein is the Asp-rich region of the C-terminal region.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
CASQ2 can be anchored into the membrane of SR thanks to two integral proteins: the triadin and the junctin.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">PMID:15731387</ref> triadin as well as juctin can bind to CASQ2 because of its KEKE motif between the amino acids 210 and 224 for the triadin.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref> The binding site of CASQ2 for the both protein is the Asp-rich region of the C-terminal region.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
Triadin and Junctin interact with Ryanodin Receptor (RyR).<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
Triadin and Junctin interact with Ryanodin Receptor (RyR).<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
The binding site of CASQ2 to RyR is unknow.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
The binding site of CASQ2 to RyR is unknow.<ref name="Regulation of Ryanodine Receptors by Calsequestrin: Effect of High Luminal Ca2+ and Phosphorylation (Beard et Al., 2005)">http://www.ncbi.nlm.nih.gov/pubmed/15731387</ref>
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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>
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>
<!-- 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: Calsequestrin and the calcium release channel of skeletal and cardiac muscle (Beard et Al., 2004) Lien: http://www.ncbi.nlm.nih.gov/pubmed/15050380 -->
There are <scene name='56/568018/Alpha_helix/1'>12 alpha helix</scene> and <scene name='56/568018/Beta_sheet/2'>15 beta sheet</scene>.
<scene name='56/568018/Acidic_amino_acids/1'>The acidics amino acids</scene> can bind the Ca2+ especially the <scene name='56/568018/Glu/2'>glutamate</scene> and the <scene name='56/568018/Asp/3'>aspartate</scene>.


The Ct domain is highly implicated in the Ca2+ bounds.
The Ca2+ is bound with the interaction of at least 2 acidic amino acids (glutamate or aspartate). These amino acids are in the external part of the protein. When Ca2+ binds to these amino acids there is a structural change which increase the number of alpha helix. Without Ca2+, there are 10-13% of alpha helix but in presence of Ca2+ there 20->35% of alpha helix.
The N-term domain is implicated in front-to-front dimer interactions. While the C-term domain is involved in back-to-back dimer interactions.
</StructureSection>
</StructureSection>
== References ==
== References ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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