Abstract
Excitation-contraction coupling in skeletal muscle requires the release of intracellular calcium ions (Ca2+) through ryanodine receptor (RyR1) channels in the sarcoplasmic reticulum. Half of the RyR1 channels are activated by voltage-dependent Ca2+ channels in the plasma membrane. In planar lipid bilayers, RyR1 channels exhibited simultaneous openings and closings, termed "coupled gating." Addition of the channel accessory protein FKBP12 induced coupled gating, and removal of FKBP12 uncoupled channels. Coupled gating provides a mechanism by which RyR1 channels that are not associated with voltage-dependent Ca2+ channels can be regulated.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Calcium / metabolism*
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Calcium Channels / metabolism
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Carrier Proteins / metabolism
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Cell Line
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DNA-Binding Proteins / metabolism
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Heat-Shock Proteins / metabolism
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Ion Channel Gating* / drug effects
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Lipid Bilayers
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Muscle, Skeletal / metabolism
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Polyenes / pharmacology
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Probability
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Rabbits
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Recombinant Proteins / metabolism
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Ryanodine / metabolism
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Ryanodine Receptor Calcium Release Channel / metabolism*
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Sarcoplasmic Reticulum / metabolism*
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Sirolimus
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Spodoptera
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Tacrolimus Binding Proteins
Substances
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Calcium Channels
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Carrier Proteins
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DNA-Binding Proteins
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Heat-Shock Proteins
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Lipid Bilayers
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Polyenes
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Recombinant Proteins
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Ryanodine Receptor Calcium Release Channel
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Ryanodine
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Tacrolimus Binding Proteins
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Calcium
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Sirolimus