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

doi:10.1016/S1097-2765(00)00041-1

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

Department of Oral Biology

Research output: Contribution to journal › Article › peer-review

141 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	421-431
Number of pages	11
Journal	Molecular Cell
Volume	6
Issue number	2
DOIs	https://doi.org/10.1016/S1097-2765(00)00041-1
Publication status	Published - 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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10.1016/S1097-2765(00)00041-1

Cite this

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title = "Gating of store-operated channels by conformational coupling to ryanodine receptors",

abstract = "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.",

author = "Kiselyov, {Kirill I.} and Shin, {Dong Min} and Yaming Wang and Pessah, {Isaac N.} and Allen, {Paul D.} and Shmuel Muallem",

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.",

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T1 - Gating of store-operated channels by conformational coupling to ryanodine receptors

AU - Kiselyov, Kirill I.

AU - Shin, Dong Min

AU - Wang, Yaming

AU - Pessah, Isaac N.

AU - Allen, Paul D.

AU - Muallem, Shmuel

N1 - 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.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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