Molecular Cloning and Functional Expression of KCNQ5, a Potassium Channel Subunit That May Contribute to Neuronal M-current Diversity
We have isolated KCNQ5, a novel human member of the KCNQ potassium channel gene family that is differentially expressed in subregions of the brain and in skeletal muscle. When expressed inXenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K+-selective currents that displayed a mar...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-07, Vol.275 (29), p.22395-22400 |
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| container_title | The Journal of biological chemistry |
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| creator | Lerche, Christian Scherer, Constanze R. Seebohm, Guiscard Derst, Christian Wei, Aguan D. Busch, Andreas E. Steinmeyer, Klaus |
| description | We have isolated KCNQ5, a novel human member of the KCNQ potassium channel gene family that is differentially expressed in subregions of the brain and in skeletal muscle. When expressed inXenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K+-selective currents that displayed a marked inward rectification at positive membrane voltages. KCNQ5 currents were insensitive to the K+ channel blocker tetraethylammonium but were strongly inhibited by the selective M-current blocker linopirdine. Upon coexpression with the structurally related KCNQ3 channel subunit, current amplitudes increased 4–5-fold. Compared with homomeric KCNQ5 currents, KCNQ3/KCNQ5 currents also displayed slower activation kinetics and less inward rectification, indicating that KCNQ5 combined with KCNQ3 to form functional heteromeric channel proteins. This functional interaction between KCNQ5 and KCNQ3, a component of the M-channel, suggests that KCNQ5 may contribute to a diversity of heteromeric channels underlying native neuronal M-currents. |
| doi_str_mv | 10.1074/jbc.M002378200 |
| format | Article |
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When expressed inXenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K+-selective currents that displayed a marked inward rectification at positive membrane voltages. KCNQ5 currents were insensitive to the K+ channel blocker tetraethylammonium but were strongly inhibited by the selective M-current blocker linopirdine. Upon coexpression with the structurally related KCNQ3 channel subunit, current amplitudes increased 4–5-fold. Compared with homomeric KCNQ5 currents, KCNQ3/KCNQ5 currents also displayed slower activation kinetics and less inward rectification, indicating that KCNQ5 combined with KCNQ3 to form functional heteromeric channel proteins. This functional interaction between KCNQ5 and KCNQ3, a component of the M-channel, suggests that KCNQ5 may contribute to a diversity of heteromeric channels underlying native neuronal M-currents.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M002378200</identifier><identifier>PMID: 10787416</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Cloning, Molecular ; Genetic Variation ; Humans ; Ion Transport ; KCNQ Potassium Channels ; KCNQ5 gene ; Molecular Sequence Data ; Neurons - physiology ; Potassium - metabolism ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated ; Sequence Alignment ; Xenopus</subject><ispartof>The Journal of biological chemistry, 2000-07, Vol.275 (29), p.22395-22400</ispartof><rights>2000 © 2000 ASBMB. 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When expressed inXenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K+-selective currents that displayed a marked inward rectification at positive membrane voltages. KCNQ5 currents were insensitive to the K+ channel blocker tetraethylammonium but were strongly inhibited by the selective M-current blocker linopirdine. Upon coexpression with the structurally related KCNQ3 channel subunit, current amplitudes increased 4–5-fold. Compared with homomeric KCNQ5 currents, KCNQ3/KCNQ5 currents also displayed slower activation kinetics and less inward rectification, indicating that KCNQ5 combined with KCNQ3 to form functional heteromeric channel proteins. This functional interaction between KCNQ5 and KCNQ3, a component of the M-channel, suggests that KCNQ5 may contribute to a diversity of heteromeric channels underlying native neuronal M-currents.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cloning, Molecular</subject><subject>Genetic Variation</subject><subject>Humans</subject><subject>Ion Transport</subject><subject>KCNQ Potassium Channels</subject><subject>KCNQ5 gene</subject><subject>Molecular Sequence Data</subject><subject>Neurons - physiology</subject><subject>Potassium - metabolism</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - metabolism</subject><subject>Potassium Channels, Voltage-Gated</subject><subject>Sequence Alignment</subject><subject>Xenopus</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EokNhyxJ5gViRwXbiPJYotAXRKSCKxM5ynOvGVWIPfpTOD-B_Y0gl2CC8sXz0naN7fRB6SsmWkqZ6dT2o7Y4QVjYtI-Qe2lDSlkXJ6df7aJN1WnSMt0foUQjXJJ-qow_RUba2TUXrDfqxczOoNEuP-9lZY6-wtCM-TVZF46yc8cnt3kMI-YGdxu_7i0_8JZb4o4syq2nB_SSthRl_TkOyJuLLSUa8kwfcOxu9GVIEHB2-gOR_B-4KlbwHG_EbcwM-mHh4jB5oOQd4cncfoy-nJ5f92-L8w9m7_vV5oTglsYBhHGpgVddVUrNal4RzTWilOylZy_NuHWk4VbxrWy0zqcqRgZaDlo2sSV0eoxdr7t67bwlCFIsJCuZZWnApiIayqq4J_S9Im7rtKGszuF1B5V0IHrTYe7NIfxCUiF8NidyQ-NNQNjy7S07DAuNf-FpJBp6vwGSupu_GgxiMUxMsgjVcsE4wVnY8Y-2KQf6vGwNeBGXAKhizRUUxOvOvEX4Ca4CrtA</recordid><startdate>20000721</startdate><enddate>20000721</enddate><creator>Lerche, Christian</creator><creator>Scherer, Constanze R.</creator><creator>Seebohm, Guiscard</creator><creator>Derst, Christian</creator><creator>Wei, Aguan D.</creator><creator>Busch, Andreas E.</creator><creator>Steinmeyer, Klaus</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000721</creationdate><title>Molecular Cloning and Functional Expression of KCNQ5, a Potassium Channel Subunit That May Contribute to Neuronal M-current Diversity</title><author>Lerche, Christian ; 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When expressed inXenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K+-selective currents that displayed a marked inward rectification at positive membrane voltages. KCNQ5 currents were insensitive to the K+ channel blocker tetraethylammonium but were strongly inhibited by the selective M-current blocker linopirdine. Upon coexpression with the structurally related KCNQ3 channel subunit, current amplitudes increased 4–5-fold. Compared with homomeric KCNQ5 currents, KCNQ3/KCNQ5 currents also displayed slower activation kinetics and less inward rectification, indicating that KCNQ5 combined with KCNQ3 to form functional heteromeric channel proteins. 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| subjects | Amino Acid Sequence Animals Cloning, Molecular Genetic Variation Humans Ion Transport KCNQ Potassium Channels KCNQ5 gene Molecular Sequence Data Neurons - physiology Potassium - metabolism Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated Sequence Alignment Xenopus |
| title | Molecular Cloning and Functional Expression of KCNQ5, a Potassium Channel Subunit That May Contribute to Neuronal M-current Diversity |
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