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Volume 271, Number 46, Issue of November 15, 1996 pp. 28837-28843
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

cAMP-dependent Phosphorylation of Two Sites in the alpha  Subunit of the Cardiac Sodium Channel

(Received for publication, July 23, 1996, and in revised form, September 6, 1996)

Brian J. Murphy , John Rogers , Andrew P. Perdichizzi , Anita A. Colvin and William A. Catterall

From the Department of Pharmacology, University of Washington, Seattle, Washington 98195-7280

The voltage-sensitive Na+ channel is responsible for generating action potentials in the heart which are critical for coordinated cardiac muscle contraction. Cardiac Na+ channels are regulated by cAMP-dependent phosphorylation, but the sites of phosphorylation are not known. Using mammalian cells expressing the rat cardiac Na+ channel (rH1) alpha  subunit and site-specific antibodies, we have shown that the alpha  subunit of rat heart Na+ channel is phosphorylated selectively by cAMP-dependent protein kinase (PKA) in vitro and in intact cells. Analysis of the sites of phosphorylation by two-dimensional phosphopeptide mapping and site-directed mutagenesis of fusion proteins revealed that the cardiac alpha  subunit is phosphorylated selectively in vitro by PKA on Ser526 and Ser529 in the intracellular loop connecting homologous domains I and II (LI-II). These two residues were phosphorylated in intact cells expressing the rH1 alpha  subunit when PKA was activated. Our results define a different pattern of phosphorylation of LI-II of cardiac and brain Na+ channels and implicate phosphorylation of Ser526 and Ser529 in the differential regulation of cardiac and brain Na+ channels by PKA.


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