The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
Open accessAbstract
Ryanodine receptors have recently been shown to be the Ca2+ release channels of sarcoplasmic reticulum in both cardiac muscle and skeletal muscle. Several regulatory sites are postulated to exist on these receptors, but to date, none have been definitively identified. In the work described here, we localize one of these sites by showing that the cardiac isoform of the ryanodine receptor is a preferred substrate for multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase). Phosphorylation by CaM kinase occurs at a single site encompassing serine 2809. Antibodies generated to this site react only with the cardiac isoform of the ryanodine receptor, and immunoprecipitate only cardiac [3H]ryanodine-binding sites. When cardiac junctional sarcoplasmic reticulum vesicles or partially purified ryanodine receptors are fused with planar bilayers, phosphorylation at this site activates the Ca2+ channel. In tissues expressing the cardiac isoform of the ryanodine receptor, such as heart and brain, phosphorylation of the Ca2+ release channel by CaM kinase may provide a unique mechanism for regulating intracellular Ca2+ release.
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Cites
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Cited by
Wehrens, X. H. T., Lehnart, S. E., Reiken, S. R., & Marks, A. R. (2004) · Circulation Research · doi:10.1161/01.res.0000125626.33738.e2 · Cited by 623
Modulation of the Ryanodine Receptor and Intracellular Calcium
Zalk, R., Lehnart, S. E., & Marks, A. R. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.053105.094237 · Cited by 371
INTRACELLULAR CALCIUM RELEASE AND CARDIAC DISEASE
Wehrens, X. H. T., Lehnart, S. E., & Marks, A. R. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.040403.114521 · Cited by 355
Calcium Signaling in Cardiac Myocytes
Fearnley, C. J., Roderick, H. L., & Bootman, M. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004242 · Cited by 339
Computational biology in the study of cardiac ion channels and cell electrophysiology
Rudy, Y., & Silva, J. R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004227 · Cited by 260
Metadata
- Authors
- Witcher, D. R., Kovacs, R. J., Schulman, H., Cefali, D. C., & Jones, L. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-06
- Volume
- 266
- Issue
- 17
- Pages
- 11144-11152
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1483351525
- Cited by
- 507
- References
- 36
- FWCI
- 6.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Witcher, D. R., Kovacs, R. J., Schulman, H., Cefali, D. C., & Jones, L. R. (1991). Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)99140-4
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
