Two Regions of the Ryanodine Receptor Involved in Coupling withl-Type Ca2+ Channels*

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) Nature325, 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 tol-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.

• Publication year

  1998

• Venue

  Journal of Biological Chemistry

• Publication date

  1998-05-29

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/jbc.273.22.13403PMID 9593671
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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