Subunit stoichiometry of a heteromultimeric G protein-coupled inward- rectifier K+ channel

Scott K. Silverman; Henry A. Lester; Dennis A. Dougherty

doi:10.1074/jbc.271.48.30524

Subunit stoichiometry of a heteromultimeric G protein-coupled inward- rectifier K⁺ channel

Scott K. Silverman, Henry A. Lester, Dennis A. Dougherty

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

Abstract

We investigated the stoichiometry of the heteromultimeric G protein- coupled inward-rectifier K⁺ channel (GIRK) formed from GIRK1 and GIRK4 subunits. Multimeric GIRK constructs with several concatenated channel subunits were expressed in Xenopus oocytes. Coexpression of various trimeric constructs with different monomers clearly showed that the functional channel has stoichiometry (GIRK1)₂(GIRK4)₂. Efforts to establish a preferred arrangement of subunits around the channel pore suggest that more than one arrangement may be viable.

Original language	English (US)
Pages (from-to)	30524-30528
Number of pages	5
Journal	Journal of Biological Chemistry
Volume	271
Issue number	48
DOIs	https://doi.org/10.1074/jbc.271.48.30524
State	Published - 1996
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.271.48.30524

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abstract = "We investigated the stoichiometry of the heteromultimeric G protein- coupled inward-rectifier K+ channel (GIRK) formed from GIRK1 and GIRK4 subunits. Multimeric GIRK constructs with several concatenated channel subunits were expressed in Xenopus oocytes. Coexpression of various trimeric constructs with different monomers clearly showed that the functional channel has stoichiometry (GIRK1)2(GIRK4)2. Efforts to establish a preferred arrangement of subunits around the channel pore suggest that more than one arrangement may be viable.",

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AU - Lester, Henry A.

AU - Dougherty, Dennis A.

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AB - We investigated the stoichiometry of the heteromultimeric G protein- coupled inward-rectifier K+ channel (GIRK) formed from GIRK1 and GIRK4 subunits. Multimeric GIRK constructs with several concatenated channel subunits were expressed in Xenopus oocytes. Coexpression of various trimeric constructs with different monomers clearly showed that the functional channel has stoichiometry (GIRK1)2(GIRK4)2. Efforts to establish a preferred arrangement of subunits around the channel pore suggest that more than one arrangement may be viable.

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