Literature DB >> 10983988

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

K I Kiselyov1, D M Shin, Y Wang, I N Pessah, P D Allen, S Muallem.   

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.

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Year:  2000        PMID： 10983988     DOI： 10.1016/s1097-2765(00)00041-1

Source DB:  PubMed          Journal:  Mol Cell        ISSN： 1097-2765            Impact factor:   17.970


  42 in total

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Review 8.  Calcium entry in skeletal muscle.

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9.  Activation of ryanodine receptors induces calcium influx in a neuroblastoma cell line lacking calcium influx factor activity.

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Journal:  Biochem J       Date:  2005-03-01       Impact factor: 3.857

Review 10.  Homer and the ryanodine receptor.

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