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

Authors: M A Post, G E Kirsch, A M Brown

Journal, date & volume: FEBS Lett., 1996 Dec 9 , 399, 177-82

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/8980147

Abstract
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 alpha-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.