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

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

Research output: Contribution to journalArticlepeer-review

141 Citations (Scopus)


We report here that RyRs interact with and gate the store-operated hTrp3 and I(crac) channels. This gating contributes to activation of hTrp3 and I(crac) 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.

Original languageEnglish
Pages (from-to)421-431
Number of pages11
JournalMolecular Cell
Issue number2
Publication statusPublished - 2000

Bibliographical note

Funding Information:
We thank Mike Zhu for providing us with the parental HEK293 and the T 3 clones and Karen Miller for expert administrative assistance. This work was supported by the National Institutes of Health.

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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