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. 1995 Jun;14(6):1303-9.
doi: 10.1016/0896-6273(95)90277-5.

Subunit composition of minK potassium channels

K W Wang  1 , S A Goldstein
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Free article

Subunit composition of minK potassium channels

K W Wang et al. Neuron. 1995 Jun.
Free article

Abstract

Expression of minK protein in Xenopus oocytes induces a slowly activating, voltage-dependent, potassium-selective current. Point mutations in minK that alter current gating kinetics, ion selectivity, pharmacology, and response to protein kinase C all support the notion that minK is a structural protein for a channel-type transporter. Yet, minK has just 130 amino acids and a single transmembrane domain. Though larger cloned potassium channels form functional channels through tetrameric subunit association, the subunit composition of minK is unknown. Subunit stoichiometry was determined by coexpression of wild-type minK and a dominant lethal point mutant of minK, which reaches the plasma membrane but passes no current. The results support a model for complete minK potassium channels in which just two minK monomers are present, with other, as yet unidentified, non-minK subunits.

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