ArticleBiophysical journal2002
Role of the proposed pore-forming segment of the Ca2+ release channel (ryanodine receptor) in ryanodine interaction.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- A Comparative Perspective on Functionally-Related, Intracellular Calcium Channels: The Insect Ryanodine and Inositol 1,4,5-Trisphosphate Receptors.Biomolecules · 2021Review
- The central domain of cardiac ryanodine receptor governs channel activation, regulation, and stability.The Journal of biological chemistry · 2020Article
- Intracellular Calcium Mobilization Is Required for Sonic Hedgehog Signaling.Developmental cell · 2018Article
- Mapping Ryanodine Binding Sites in the Pore Cavity of Ryanodine Receptors.Biophysical journal · 2017Article
- The Cytoplasmic Region of Inner Helix S6 Is an Important Determinant of Cardiac Ryanodine Receptor Channel Gating.The Journal of biological chemistry · 2016Article
- Approaching ryanodine receptor therapeutics from the calcin angle.The Journal of general physiology · 2016Article
- Mechanisms of SR calcium release in healthy and failing human hearts.Biophysical reviews · 2015Article
- Article
- Type 2 ryanodine receptors are highly sensitive to alcohol.FEBS letters · 2014Article
- Patch-clamp electrophysiology of intracellular Ca2+ channels.Cold Spring Harbor protocols · 2013Article
- The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations and Shaker B inactivation peptides.The Journal of general physiology · 2012Article
- Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites.PloS one · 2011Article
- Unitary Ca(2+) current through recombinant type 3 InsP(3) receptor channels under physiological ionic conditions.The Journal of general physiology · 2010Article
- Linking structure to function: Recent lessons from inositol 1,4,5-trisphosphate receptor mutagenesis.Cell calcium · 2010Review
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
- Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor.Biophysical journal · 2009Article
- The ryanodine receptor pore blocker neomycin also inhibits channel activity via a previously undescribed high-affinity Ca(2+) binding site.The Journal of membrane biology · 2007Article
- Localization of an NH(2)-terminal disease-causing mutation hot spot to the "clamp" region in the three-dimensional structure of the cardiac ryanodine receptor.The Journal of biological chemistry · 2007Article
- Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.Biophysical journal · 2006Article
- Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor.Biophysical journal · 2005Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In earlier studies we showed that point mutations introduced into the proposed pore-forming segment, GVRAGGGIGD (amino acids 4820-4829), of the mouse cardiac ryanodine receptor reduced or abolished high affinity [3H]ryanodine binding. Here we investigate the effects of these mutations on the affinity and dissociation properties of [3H]ryanodine binding and on ryanodine modification of the ryanodine receptor channel at the single channel and whole cell levels. Scatchard analysis and dissociation studies reveal that mutation G4824A decreases the equilibrium dissociation constant (K(d)) and the dissociation rate constant (k(off)), whereas mutations G4828A and D4829A increase the K(d) and k(off) values. The effect of ryanodine on single G4828A and D4829A mutant channels is reversible on the time scale of single channel experiments, in contrast to the irreversible effect of ryanodine on single wild-type channels. Ryanodine alone is able to induce a large and sustained Ca2+ release in HEK293 cells transfected with the R4822A or G4825A mutant cDNA at the resting cytoplasmic Ca2+ but causes little or no Ca2+ release in cells transfected with the wild-type cDNA. Mutation G4826C diminishes the functional effect of ryanodine on Ca2+ release but spares caffeine-induced Ca2+ release in HEK293 cells. Co-expression of the wild-type and G4826C mutant proteins produces single channels that interact with ryanodine reversibly and display altered conductance and ryanodine response. These results are consistent with the view that the proposed pore-forming segment is a critical determinant of ryanodine interaction. A putative model of ryanodine-ryanodine receptor interaction is proposed.
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