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J Biol Chem, Vol. 273, Issue 22, 13403-13406, May 29, 1998
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From the Ryanodine receptors (RyRs) are
present in the endoplasmic reticulum of virtually every cell type and
serve critical roles, including excitation-contraction (EC) coupling in
muscle cells. In skeletal muscle the primary control of RyR-1 (the
predominant skeletal RyR isoform) occurs via an interaction with
plasmalemmal dihydropyridine receptors (DHPRs), which function as both
voltage sensors for EC coupling and as L-type
Ca2+ channels (Rios, E., and Brum, G. (1987) Nature
325, 717-720). In addition to "receiving" the EC coupling
signal from the DHPR, RyR-1 also "transmits" a retrograde signal
that enhances the Ca2+ channel activity of the DHPR (Nakai,
J., Dirksen, R. T., Nguyen, H. T., Pessah, I. N., Beam,
K. G., and Allen, P. D. (1996) Nature 380, 72-76). A similar kind of retrograde signaling (from RyRs to
L-type Ca2+ channels) has also been reported in
neurons (Chavis, P., Fagni, L., Lansman, J. B., and Bockaert, J. (1996) Nature 382, 719-722). To investigate the molecular
mechanism of reciprocal signaling, we constructed cDNAs encoding
chimeras of RyR-1 and RyR-2 (the predominant cardiac RyR isoform) and
expressed them in dyspedic myotubes, which lack an endogenous RyR-1. We
found that a chimera that contained residues 1,635-2,636 of RyR-1 both
mediated skeletal-type EC coupling and enhanced Ca2+
channel function, whereas a chimera containing adjacent RyR-1 residues
(2,659-3,720) was only able to enhance Ca2+ channel
function. These results demonstrate that two distinct regions are
involved in the reciprocal interactions of RyR-1 with the skeletal
DHPR.
Department of Information Physiology,
National Institute for Physiological Sciences, Myodaiji-cho, Okazaki,
444, Japan, the § Department of Veterans Affairs, Palo Alto,
Department of Neurology and Neurological Sciences, Stanford University
School of Medicine, Stanford, California 94305, the ¶ Department
of Anesthesiology, Brigham and Women's Hospital, Boston, Massachusetts
02115, and the Department of Anatomy and Neurobiology, College
of Veterinary Medicine and Biomedical Sciences, Colorado State
University, Fort Collins, Colorado 80523-1670
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P. Leong and D. H. MacLennan The Cytoplasmic Loops between Domains II and III and Domains III and IV in the Skeletal Muscle Dihydropyridine Receptor Bind to a Contiguous Site in the Skeletal Muscle Ryanodine Receptor J. Biol. Chem., November 6, 1998; 273(45): 29958 - 29964. [Abstract] [Full Text] [PDF]
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S. Sencer, R. V. L. Papineni, D. B. Halling, P. Pate, J. Krol, J.-Z. Zhang, and S. L. Hamilton Coupling of RYR1 and L-type Calcium Channels via Calmodulin Binding Domains J. Biol. Chem., October 5, 2001; 276(41): 38237 - 38241. [Abstract] [Full Text] [PDF]
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T. Yamamoto and N. Ikemoto T-tubule Depolarization-induced Local Events in the Ryanodine Receptor, as Monitored with the Fluorescent Conformational Probe Incorporated by Mediation of Peptide A J. Biol. Chem., January 4, 2002; 277(2): 984 - 992. [Abstract] [Full Text] [PDF]
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M. Samso and T. Wagenknecht Apocalmodulin and Ca2+-Calmodulin Bind to Neighboring Locations on the Ryanodine Receptor J. Biol. Chem., January 4, 2002; 277(2): 1349 - 1353. [Abstract] [Full Text] [PDF]
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Z. Liu, J. Zhang, M. R. Sharma, P. Li, S. R. W. Chen, and T. Wagenknecht Three-dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus PNAS, May 22, 2001; 98(11): 6104 - 6109. [Abstract] [Full Text] [PDF]
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