Calsequestrin. Structure,function, and evolution |
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Affiliation: | 1. Department of Cardiothoracic Surgery, Lund University, and Skåne University Hospital, Lund, Sweden;2. Department Physiology and Pharmacology, Karolinska Institutet, v Eulers v 8, Stockholm, Sweden;3. H. Lundbeck A/S, DK-2500, Valby, Copenhagen, Denmark |
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Abstract: | Calsequestrin is the major Ca2+ binding protein in the sarcoplasmic reticulum (SR), serves as the main Ca2+ storage and buffering protein and is an important regulator of Ca2+ release channels in both skeletal and cardiac muscle. It is anchored at the junctional SR membrane through interactions with membrane proteins and undergoes reversible polymerization with increasing Ca2+ concentration. Calsequestrin provides high local Ca2+ at the junctional SR and communicates changes in luminal Ca2+ concentration to Ca2+ release channels, thus it is an essential component of excitation-contraction coupling. Recent studies reveal new insights on calsequestrin trafficking, Ca2+ binding, protein evolution, protein-protein interactions, stress responses and the molecular basis of related human muscle disease, including catecholaminergic polymorphic ventricular tachycardia (CPVT). Here we provide a comprehensive overview of calsequestrin, with recent advances in structure, diverse functions, phylogenetic analysis, and its role in muscle physiology, stress responses and human pathology. |
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Keywords: | Calcium binding protein Sarcoplasmic reticulum Calcium storage Excitation-contraction coupling Ryanodine receptor Stress sensor |
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