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min K channels form by assembly of at least 14 subunits.

Authors: Tzounopoulos, T  Guy, H R  Durell, S  Adelman, J P  Maylie, J 
Citation: Tzounopoulos T, etal., Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9593-7.
Pubmed: (View Article at PubMed) PMID:7568179

Injection of min K mRNA into Xenopus oocytes results in expression of slowly activating voltage-dependent potassium channels, distinct from those induced by expression of other cloned potassium channels. The min K protein also differs in structure, containing only a single predicted transmembrane domain. While it has been demonstrated that all other cloned potassium channels form by association of four independent subunits, the number of min K monomers which constitute a functional channel is unknown. In rat min K, replacement of Ser-69 by Ala (S69A) causes a shift in the current-voltage (I-V) relationship to more depolarized potentials; currents are not observed at potentials negative to 0 mV. To determine the subunit stoichiometry of min K channels, wild-type and S69A subunits were coexpressed. Injections of a constant amount of wild-type mRNA with increasing amounts of S69A mRNA led to potassium currents of decreasing amplitude upon voltage commands to -20 mV. Applying a binomial distribution to the reduction of current amplitudes as a function of the different coinjection mixtures yielded a subunit stoichiometry of at least 14 monomers for each functional min K channel. A model is presented for how min K subunits may form a channel.

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RGD Object Information
RGD ID: 12910723
Created: 2017-06-22
Species: All species
Last Modified: 2017-06-22
Status: ACTIVE



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