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Originally published In Press as doi:10.1074/jbc.M100856200 on March 1, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16931-16935, May 18, 2001
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FKBP12 Binding Modulates Ryanodine Receptor Channel Gating*

Marta Gaburjakova, Jana Gaburjakova, Steven Reiken, Fannie Huang, Steven O. Marx, Nora Rosemblit, and Andrew R. MarksDagger

From the Center for Molecular Cardiology and Departments of Medicine and Pharmacology, Columbia University College of Physicians and Surgeons, New York, New York 10032

The ryanodine receptor (RyR1)/calcium release channel on the sarcoplasmic reticulum of skeletal muscle is comprised of four 565,000-dalton RyR1s, each of which binds one FK506 binding protein (FKBP12). RyR1 is required for excitation-contraction coupling in skeletal muscle. FKBP12, a cis-trans peptidyl-prolyl isomerase, is required for the normal gating of the RyR1 channel. In the absence of FKBP12, RyR1 channels exhibit increased gating frequency, suggesting that FKBP12 "stabilizes" the channel in the open and closed states. We now show that substitution of a Gly, Glu, or Ile for Val2461 in RyR1 prevents FKBP12 binding to RyR1, resulting in channels with increased gating frequency. In the case of the V2461I mutant RyR1, normal channel function can be restored by adding FKBP12.6, an isoform of FKBP12. These data identify Val2461 as a critical residue required for FKBP12 binding to RyR1 and demonstrate the functional role for FKBP12 in the RyR1 channel complex.


* This work was supported by National Institutes of Health Grants RO1 HL61503, RO1 HL56180, RO1 AI39794, and RO3 TW00949 (to A. R. M.), the American Heart Association (to A. R. M. and S. O. M.), the Whitaker Foundation (to S. R.), and the Richard and Lynne Kaiser Family Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Doris Duke Distinguished Clinical Scientist. To whom correspondence should be addressed: Center for Molecular Cardiology, Box 65, Columbia University College of Physicians and Surgeons, Rm. 9-401, 630 W. 168th St., New York, NY 10032. Tel.: 212-305-0270; Fax: 212-305-3690; E-mail: arm42@columbia.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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