Transmembrane Redox Sensor of Ryanodine Receptor Complex
نویسندگان
چکیده
منابع مشابه
Redox sensing properties of the ryanodine receptor complex.
The release mechanism regulating SR Ca2+ homeostasis is significantly more sensitive than the uptake mechanisms. The exquisite sensitivity exhibited by ryanodine-sensitive Ca2+ channel complexes (i.e., ryanodine receptors, RyRs) to functional perturbation by chemically diverse sulfhydryl-modifying compounds can include phases of activation and inhibition that are dependent on the concentration ...
متن کاملRedox regulation of the ryanodine receptor/calcium release channel.
The RyR (ryanodine receptor)/calcium release channel contains a number of highly reactive thiol groups that endow it with redox sensitivity. In general, oxidizing conditions favour channel opening, while reducing conditions have the opposite effect. Thiol modification affects the channel sensitivity to its principal effectors, Ca2+, Mg2+ and ATP, and alters RyR protein interactions. Here, we gi...
متن کاملLanthanides Report Calcium Sensor in the Vestibule of Ryanodine Receptor.
Ca2+ regulates ryanodine receptor's (RyR) activity through an activating and an inhibiting Ca2+-binding site located on the cytoplasmic side of the RyR channel. Their altered sensitivity plays an important role in the pathology of malignant hyperthermia and heart failure. We used lanthanide ions (Ln3+) as probes to investigate the Ca2+ sensors of RyR, because they specifically bind to Ca2+-bind...
متن کاملResidue Gln within a Predicted Transmembrane Sequence of the Ca Release Channel (Ryanodine Receptor) Is Critical for Ryanodine Interaction*
From the ‡Cardiovascular Research Group, Departments of Physiology and Biophysics and of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada, the §Department of Chemistry, University of Sherbrooke, Sherbrooke, Quebec J1K 2R1, Canada, the ¶Department of Biochemistry, University of Nevada School of Medicine, Reno, Nevada 89557, and Cardiac Medicine, Nationa...
متن کاملResidue Gln4863 within a predicted transmembrane sequence of the Ca2+ release channel (ryanodine receptor) is critical for ryanodine interaction.
Despite the pivotal role of ryanodine in ryanodine receptor (RyR) research, the molecular basis of ryanodine-RyR interaction remains largely undefined. We investigated the role of the proposed transmembrane helix TM10 in ryanodine interaction and channel function. Each amino acid residue within the TM10 sequence, 4844IIFDITFFFFVIVILLAIIQGLII4867, of the mouse RyR2 was mutated to either alanine ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.c000523200