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Calsequestrin, a key protein in striated muscle health and disease.
- Source :
-
Journal of muscle research and cell motility [J Muscle Res Cell Motil] 2021 Jun; Vol. 42 (2), pp. 267-279. Date of Electronic Publication: 2020 Jun 02. - Publication Year :
- 2021
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Abstract
- Calsequestrin (CASQ) is the most abundant Ca <superscript>2+</superscript> binding protein localized in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. The genome of vertebrates contains two genes, CASQ1 and CASQ2. CASQ1 and CASQ2 have a high level of homology, but show specific patterns of expression. Fast-twitch skeletal muscle fibers express only CASQ1, both CASQ1 and CASQ2 are present in slow-twitch skeletal muscle fibers, while CASQ2 is the only protein present in cardiomyocytes. Depending on the intraluminal SR Ca <superscript>2+</superscript> levels, CASQ monomers assemble to form large polymers, which increase their Ca <superscript>2+</superscript> binding ability. CASQ interacts with triadin and junctin, two additional SR proteins which contribute to localize CASQ to the junctional region of the SR (j-SR) and also modulate CASQ ability to polymerize into large macromolecular complexes. In addition to its ability to bind Ca <superscript>2+</superscript> in the SR, CASQ appears also to be able to contribute to regulation of Ca <superscript>2+</superscript> homeostasis in muscle cells. Both CASQ1 and CASQ2 are able to either activate and inhibit the ryanodine receptors (RyRs) calcium release channels, likely through their interactions with junctin and triadin. Additional evidence indicates that CASQ1 contributes to regulate the mechanism of store operated calcium entry in skeletal muscle via a direct interaction with the Stromal Interaction Molecule 1 (STIM1). Mutations in CASQ2 and CASQ1 have been identified, respectively, in patients with catecholamine-induced polymorphic ventricular tachycardia and in patients with some forms of myopathy. This review will highlight recent developments in understanding CASQ1 and CASQ2 in health and diseases.<br /> (© 2020. Springer Nature Switzerland AG.)
Details
- Language :
- English
- ISSN :
- 1573-2657
- Volume :
- 42
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Journal of muscle research and cell motility
- Publication Type :
- Academic Journal
- Accession number :
- 32488451
- Full Text :
- https://doi.org/10.1007/s10974-020-09583-6