The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
FK506 binding protein associated with the calcium release channel (ryanodine receptor).
Open accessAbstract
The calcium release channel (CRC)/ryanodine receptor (RyRec) has been identified as the foot structure of the sarcoplasmic reticulum (SR) and provides the pathway for calcium efflux required for excitation-contraction coupling in skeletal muscle. The CRC has previously been reported to consist of four identical 565-kDa protomers. We now report the identification of a 12-kDa protein which is tightly associated with highly purified RyRec from rabbit skeletal muscle SR. N-terminal amino acid sequencing and cDNA cloning demonstrates that the 12-kDa protein from fast twitch skeletal muscle is the binding protein for the immunosuppressant drug FK506. In humans, FK506 binds to the 12-kDa FK506-binding protein (FKBP12) and blocks calcium-dependent T cell activation. We find that FKBP12 and the RyRec are tightly associated in skeletal muscle SR on the basis of: 1) co-purification through sequential heparin-agarose, hydroxylapatite, and size exclusion chromatography columns; 2) coimmunoprecipitation of the RyRec and FKBP12 with anti-FKBP12 antibodies; and 3) subcellular localization of both proteins to the terminal cisternae of the SR, and not in the longitudinal tubules of SR, in fast twitch skeletal muscle. The molar ratio of FKBP12 to RyRec in highly purified RyRec preparations is approximately 1:4, indicating that one FKBP12 molecule is associated with each calcium release channel/foot structure.
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
Takeshima, H., Nishimura, S., Matsumoto, T., Ishida, H., Kangawa, K., Minamino, N., Matsuo, H., Ueda, M., Hanaoka, M., Hirose, T., et al. (1989) · Nature · doi:10.1038/339439a0 · Cited by 1,146
Cited by
Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P., & Snyder, S. H. (1994) · Cell · doi:10.1016/0092-8674(94)90570-3 · Cited by 1,509
Self-citationPhysiology of Nitric Oxide in Skeletal Muscle
Stamler, J. S., & Meissner, G. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.209 · Cited by 1,080
Coupled Gating Between Individual Skeletal Muscle Ca 2+ Release Channels (Ryanodine Receptors)
Marx, S. O., Ondrias, K., & Marks, A. R. (1998) · Science · doi:10.1126/science.281.5378.818 · Cited by 417
Self-citationModulation 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
Self-citationMinding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicity
Pessah, I. N., Cherednichenko, G., & Lein, P. J. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.10.009 · Cited by 231
Metadata
- Authors
- Jayaraman, T., Brillantes, A. M., Timerman, A. P., Fleischer, S., Erdjument-Bromage, H., Tempst, P., & Marks, A. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-05
- Volume
- 267
- Issue
- 14
- Pages
- 9474-9477
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1549665441
- Cited by
- 526
- References
- 3
- FWCI
- 8.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Jayaraman, T., Brillantes, A. M., Timerman, A. P., Fleischer, S., Erdjument-Bromage, H., Tempst, P., & Marks, A. R. (1992). FK506 binding protein associated with the calcium release channel (ryanodine receptor). Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)50114-4
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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