Kv2.1 and electrically silent Kv6.1 potassium channel subunits combine and express a novel current

Heteromultimer formation between Kv potassium channel subfamilies with the production of a novel current is reported for the first time. Protein-protein interactions between Kv2.1 and electrically silent Kv6.1 α-subunits were detected using two microelectrode voltage clamp and yeast two-hybrid measu...

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Bibliographic Details
Published in:FEBS letters 1996-12, Vol.399 (1), p.177-182
Main Authors: Post, Marc A., Kirsch, Glenn E., Brown, Arthur M.
Format: Article
Language:English
Subjects:
Animals
Heteromultimer
Patch-Clamp Techniques
Potassium channel
Potassium Channel Blockers
Potassium Channels - physiology
Recombinant Fusion Proteins - physiology
Shab Potassium Channels
Tetraethylammonium
Tetraethylammonium Compounds - pharmacology
Xenopus
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Summary:Heteromultimer formation between Kv potassium channel subfamilies with the production of a novel current is reported for the first time. Protein-protein interactions between Kv2.1 and electrically silent Kv6.1 α-subunits were detected using two microelectrode voltage clamp and yeast two-hybrid measurements. Amino terminal portions of Kv6.1 were unable to form homomultimers but interacted specifically with amino termini of Kv2.1. Xenopus oocytes co-injected with Kv6.1 and Kv2.1 cRNAs exhibited a novel current with decreased rates of deactivation, decreased sensitivity to TEA block, and a hyperpolarizing shift of the half maximal activation potential when compared to Kv2.1. Our results indicate that Kv channel subfamilies can form heteromultimeric channels and, for the first time, suggest a possible functional role for the Kv6 subfamily.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(96)01316-6