ArticleBiophysical journal2005
Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Article
- Cryo-EM Brings the Mechanisms of Activation, Inactivation, and Inhibition of Ryanodine Receptors into Focus.Advances in experimental medicine and biology · 2026Review
- EuBiophysical journal · 2023Article
- Binding of the erlin1/2 complex to the third intralumenal loop of IPThe Journal of biological chemistry · 2022Article
- Preclinical model systems of ryanodine receptor 1-related myopathies and malignant hyperthermia: a comprehensive scoping review of works published 1990-2019.Orphanet journal of rare diseases · 2020Article
- Single-channel properties of skeletal muscle ryanodine receptor pore ΔCell calcium · 2020Article
- The CaNature communications · 2020Article
- In silico assessment of the conduction mechanism of the Ryanodine Receptor 1 reveals previously unknown exit pathways.Scientific reports · 2018Article
- G4941K substitution in the pore-lining S6 helix of the skeletal muscle ryanodine receptor increases RyR1 sensitivity to cytosolic and luminal CaThe Journal of biological chemistry · 2018Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Ion-pulling simulations provide insights into the mechanisms of channel opening of the skeletal muscle ryanodine receptor.The Journal of biological chemistry · 2017Article
- Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.Cell research · 2016Article
- Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors.Journal of molecular modeling · 2016Article
- Channel Gating Dependence on Pore Lining Helix Glycine Residues in Skeletal Muscle Ryanodine Receptor.The Journal of biological chemistry · 2015Article
- Article
- Selecting ions by size in a calcium channel: the ryanodine receptor case study.Biophysical journal · 2014Article
- Pore dynamics and conductance of RyR1 transmembrane domain.Biophysical journal · 2014Article
- The ryanodine receptor store-sensing gate controls Ca2+ waves and Ca2+-triggered arrhythmias.Nature medicine · 2014Article
- Sarcoplasmic reticulum K(+) (TRIC) channel does not carry essential countercurrent during Ca(2+) release.Biophysical journal · 2013Article
- Patch-clamp electrophysiology of intracellular Ca2+ channels.Cold Spring Harbor protocols · 2013Article
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Authors and funding
5 authors.
Funding
Abstract
Sequence comparison suggests that the ryanodine receptors (RyRs) have pore architecture similar to that of the bacterial K+ channel KcsA. The lumenal loop linking the two most C-terminal transmembrane spanning segments in the RyRs has a predicted pore helix and an amino acid motif (GGGIG) similar to the selectivity filter (TVGYG) of KcsA identified by x-ray analysis. The RyRs have many negatively charged amino acid residues in the two regions linking the GGGIG motif and predicted pore helix with the two most C-terminal transmembrane spanning segments. We tested the role of these residues by generating single-site mutants, focusing on amino acid residues conserved among the mammalian RyRs. Replacement of two acidic residues immediately after the GGGIG motif in skeletal muscle ryanodine receptor (RyR1-D4899 and -E4900) with asparagine and glutamine profoundly affected ion permeation and selectivity. By comparison, mutagenesis of aspartate and glutamate residues in the putative linker regions showed a K+ conductance and selectivity for Ca2+ compared to K+ (P(Ca)/P(K)) close to wild-type. The results show that the negatively charged carboxyl oxygens of D4899 and E4900 side chains are major determinants of RyR ion conductance and selectivity.
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