A Region of the Ryanodine Receptor Critical for Excitation-Contraction Coupling in Skeletal Muscle*

@article{Yamazawa1997ARO,
  title={A Region of the Ryanodine Receptor Critical for Excitation-Contraction Coupling in Skeletal Muscle*},
  author={Toshiko Yamazawa and Hiroshi Takeshima and Misa Shimuta and Masamitsu Iino},
  journal={The Journal of Biological Chemistry},
  year={1997},
  volume={272},
  pages={8161 - 8164}
}
Ca2+ release mediated by the ryanodine receptor (RyR) regulates many important cell functions including excitation-contraction (E-C) coupling in skeletal muscle, by which membrane depolarization controls the opening of RyR via the dihydropyridine receptor. Among the three RyR subtypes, RyR-1 mediates skeletal muscle E-C coupling, whereas RyR-2 and RyR-3 cannot substitute for RyR-1. We carried out expression experiments using cultured mutant skeletal myocytes not having intrinsic intracellular… Expand
Amino Acids 1–1,680 of Ryanodine Receptor Type 1 Hold Critical Determinants of Skeletal Type for Excitation-Contraction Coupling
TLDR
Although the D2 domain of RyR1 plays a key role during EC coupling, additional region(s) from the N-terminal end of Ry ryanodine receptor as well as previously identified regions of the central portion of the receptor are needed in order to allow normal EC coupling. Expand
Two Regions of the Ryanodine Receptor Involved in Coupling withl-Type Ca2+ Channels*
TLDR
It is found that two distinct regions are involved in the reciprocal interactions of RyR-1 with the skeletal DHPR, which mediated skeletal-type EC coupling and enhanced Ca2+channel function, whereas a chimera containing adjacent Ry R-1 residues was only able to enhance Ca2+, channel function. Expand
Ryanodine receptor isoforms in excitation-contraction coupling.
TLDR
DICR and CICR in RyR1 share common properties of stimulation by concentrated solutes and modulation by luminal calcium or Ca2+, suggesting that the main difference between the two Ca2+ release mechanisms may be in the gating mechanism of the channel. Expand
Expression of the ryanodine receptor type 3 in skeletal muscle. A new partner in excitation-contraction coupling?
TLDR
New data on the expression of two isoforms of ryanodine receptors in developing skeletal muscles or in specialized adult muscles have provided initial ground to test the hypothesis that combinations of various Ca2+ release channels may be relevant to adapt the modality of Ca2- release to regulation of specific cellular functions. Expand
REGULATION OF RYANODINE RECEPTORS FROM SKELETAL AND CARDIAC MUSCLE DURING REST AND EXCITATION
  • D. Laver
  • Chemistry, Medicine
  • Clinical and experimental pharmacology & physiology
  • 2006
TLDR
Factors controlling the activity of RyRs in skeletal and cardiac muscle are reviewed with an emphasis on mechanistic insights derived from single channel recording methods. Expand
Molecular genetics of ryanodine receptors Ca2+-release channels.
TLDR
The role of protein kinases and phosphatases that, by physically interacting with RyRs, appear to play a role in the regulation of these Ca(2+)-release channels are clarified and some regulatory regions have been mapped within 3-D reconstructions. Expand
Ryanodine receptor structure, function and pathophysiology
TLDR
The ryanodine receptor is an intracellular calcium release channel located on the sarco(endo)plasmic reticulum of muscle and non-muscle cells that is regulated by intramolecular protein–protein interactions, as well as by interacting with numerous accessory proteins. Expand
Postulated role of inter-domain interaction within the ryanodine receptor in Ca(2+) channel regulation.
TLDR
It is postulate that the interaction among these regulatory domains is the central mechanism for the conformation-mediated control of the Ca(2+) channel. Expand
Bidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions
TLDR
The data support the hypotheses that the structural/functional link between RyR 1 and the skeletal muscle DHPR requires multiple interacting regions, and the D2 domain of RyR1 plays a key role in stabilizing this interaction. Expand
Membrane topology and membrane retention of the ryanodine receptor calcium release channel
TLDR
The membrane topology of RyR appears to contain an even number of transmembrane segments with a ion selectivity filter present within a region residing between the last two segments, similar to potassium channel, whose atomic structure was described recently. Expand
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TLDR
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