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