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J Biol Chem, Vol. 273, Issue 24, 14675-14678, June 12, 1998
From the Cardiovascular Research Group, Department of Medical
Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1,
Canada
We have investigated the molecular basis for
ryanodine receptor (RyR) activation by Ca2+ by using
site-directed mutagenesis together with functional assays consisting of
Ca2+ release measurements and single channel recordings in
planar lipid bilayers. We report here that a single substitution of
alanine for glutamate at position 3885 (located in the putative
transmembrane sequence M2 of the type 3 RyR) reduces the
Ca2+ sensitivity, as measured by single channel activation,
by more than 10,000-fold, without apparent changes in channel
conductance and in modulation by other ligands (e.g. ATP
and ryanodine). Co-expression of the wild type and mutant RyR proteins
results in the synthesis of single channels that have intermediate
Ca2+ sensitivities. These results suggest that the
glutamates at position 3885 of each monomer may act in a coordinated
way to form the Ca2+ sensor in the tetrameric structure
corresponding to RyR.
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