Gating of store-operated channels by conformational coupling to ryanodine receptors

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Authors: Kirill I. Kiselyov ; Dong Min Shin ; Yaming Wang ; Isaac N. Pessah ; Paul D. Allen ; Shmuel Muallem

MeSH: Barium/pharmacokinetics ; Caffeine/pharmacology ; Calcium/metabolism ; Calcium Channels/drug effects ; Calcium Channels/physiology* ; Calcium Signaling* ; Carbachol/pharmacology ; Cell Line ; Cell Membrane/physiology ; Heart/physiology ; Humans ; Ion Channel Gating/drug effects ; Ion Channel Gating/physiology* ; Muscle, Skeletal/physiology ; Patch-Clamp Techniques ; Protein Isoforms/physiology ; Recombinant Proteins/drug effects ; Recombinant Proteins/metabolism ; Ryanodine Receptor Calcium Release Channel/drug effects ; Ryanodine Receptor Calcium Release Channel/physiology* ; TRPC Cation Channels ; Transfection

Abstract: We report here that RyRs interact with and gate the store-operated hTrp3 and Icrac channels. This gating contributes to activation of hTrp3 and Icrac by agonists. Coupling of hTrp3 to IP3Rs or RyRs in the same cells was found to be mutually exclusive. Biochemical and functional evidence suggest that mutually exclusive coupling reflects clustering and segregation of hTrp3-IP3R and hTrp3-RyR complexes in plasma membrane microdomains. Gating of CCE by RyRs indicates that gating by conformational coupling is not unique to skeletal muscle but is a general mechanism for communication between events in the plasma and endoplasmic reticulum membranes.