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Volume 272, Number 45, Issue of November 7, 1997 pp. 28232-28236
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Interactions among Inactivating and Noninactivating Kvbeta Subunits, and Kvalpha 1.2, Produce Potassium Currents with Intermediate Inactivation

(Received for publication, August 11, 1997)

Eric A. Accili Dagger , Johann Kiehn , Barbara A. Wible ** and Arthur M. Brown Dagger

From the Rammelkamp Center for Research, MetroHealth Campus, and Dagger  Department of Physiology and Biophysics, ** Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44109-1998

Experiments were carried out to determine whether coinjection of Kvalpha 1.2 with inactivating and noninactivating Kvbeta subunits would produce currents with intermediate kinetics and channel complexes containing a mixture of these subunits. Upon coexpression with a saturating amount of Kvbeta 1.2 and increasing levels of a noninactivating deletion mutant of Kvbeta 1.2, we show that macroscopic Kvalpha 1.2 currents have levels of fractional inactivation and inactivation time constants that are intermediate between those obtained with either the inactivating Kvbeta 1.2 or the noninactivating Kvbeta 1.2 mutant. We also find that coexpression of Kvalpha 1.2 with saturating amounts of Kvbeta 1.2 and the deletion mutant produces a population of single channels with properties intermediate to either the inactivating or noninactivating parental phenotype. Our data can best be explained by the presence of an intermediate population of heterooligomeric channels consisting of Kvalpha 1.2 with different combinations of both types of subunits. Since Kvalpha 1.2 subunits coexist in cells with inactivating and noninactivating Kvbeta subunits, our findings suggest that heterooligomeric assembly of these subunits occurs to increase the range of K+ current kinetics and expression levels.


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