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J Biol Chem, Vol. 274, Issue 20, 13928-13932, May 14, 1999

Protein Kinase A Phosphorylation Alters Kvbeta 1.3 Subunit-mediated Inactivation of the Kv1.5 Potassium Channel

Yong-Geun KwakDagger , NingNing Hu§, Jian Wei§, Alfred L. George Jr.§, Tammy D. GrobaskiDagger , Michael M. TamkunDagger , and Katherine T. Murray§

From the Departments of § Medicine and Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6602 and the Departments of Dagger  Physiology and Biochemistry and Molecular Biology, Colorado State University, Ft. Collins, Colorado 80523

The human Kv1.5 potassium channel forms the IKur current in atrial myocytes and is functionally altered by coexpression with Kvbeta subunits. To explore the role of protein kinase A (PKA) phosphorylation in beta -subunit function, we examined the effect of PKA stimulation on Kv1.5 current following coexpression with either Kvbeta 1.2 or Kvbeta 1.3, both of which coassemble with Kv1.5 and induce fast inactivation. In Xenopus oocytes expressing Kv1.5 and Kvbeta 1.3, activation of PKA reduced macroscopic inactivation with an increase in K+ current. Similar results were obtained using HEK 293 cells which lack endogenous K+ channel subunits. These effects did not occur when Kv1.5 was coexpressed with either Kvbeta 1.2 or Kvbeta 1.3 lacking the amino terminus, suggesting involvement of this region of Kvbeta 1.3. Removal of a consensus PKA phosphorylation site on the Kvbeta 1.3 NH2 terminus (serine 24), but not alternative sites in either Kvbeta 1.3 or Kv1.5, resulted in loss of the functional effects of kinase activation. The effects of phosphorylation appeared to be electrostatic, as replacement of serine 24 with a negatively charged amino acid reduced beta -mediated inactivation, while substitution with a positively charged residue enhanced it. These results indicate that Kvbeta 1.3-induced inactivation is reduced by PKA activation, and that phosphorylation of serine 24 in the subunit NH2 terminus is responsible.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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