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The Journal of Neuroscience, December 1, 2002, 22(23):10123-10133

PKA Modulation of Kv4.2-Encoded A-Type Potassium Channels Requires Formation of a Supramolecular Complex

Laura A. Schrader1, Anne E. Anderson1, 2, Amber Mayne1, Paul J. Pfaffinger1, and John David Sweatt1

1 Division of Neuroscience and 2 Departments of Pediatrics and Neurology, Baylor College of Medicine, Houston, Texas 77030

A-type channels, encoded by the pore-forming alpha -subunits of the Kv4.x family, are particularly important in regulating membrane excitability in the CNS and the heart. Given the key role of modulation of A currents by kinases, we sought to investigate the protein structure-function relationships underlying the regulation of these currents by PKA. We have previously shown the existence of two PKA phosphorylation sites in the Kv4.2 sequence; therefore, we focused this study on the Kv4.2 primary subunit. In the present studies we made the surprising finding that PKA phosphorylation of the Kv4.2 alpha -subunit is necessary but not sufficient for channel modulation; channel modulation by PKA required the presence of an ancillary subunit, the K+ channel interacting protein (KChIP3). Therefore, these findings indicate a surprising complexity to kinase regulation of A currents, in that an interaction of two separate molecular events, alpha -subunit phosphorylation and the association of an ancillary subunit (KChIP3), are necessary for phosphorylation-dependent regulation of Kv4.2-encoded A channels by PKA. Overall, our studies indicate that PKA must of necessity act on a supramolecular complex of pore-forming alpha -subunits plus ancillary subunits to alter channel properties.

Key words: KChIP; phosphorylation; neuromodulation; Kv4.2; shal-type; PKA; heart; neuron

Copyright © 2002 Society for Neuroscience  0270-6474/02/222310123-11$05.00/0


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