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J Biol Chem, Vol. 273, Issue 19, 11745-11751, May 8, 1998
From the Rammelkamp Center of Research, Voltage-gated K+ (Kv) channels
are important in the physiology of both excitable and nonexcitable
cells. The diversity in Kv currents is reflected in multiple Kv channel
genes whose products may assemble as multisubunit heteromeric
complexes. Given the fundamental importance and diversity of Kv
channels, surprisingly little is known regarding the cellular
mechanisms regulating their synthesis, assembly, and metabolism. To
begin to dissect these processes, we have used the yeast two-hybrid
system to identify cytoplasmic regulatory molecules that interact with
Kv channel proteins. Here we report the cloning of a novel gene
encoding a Kv channel binding protein (KChAP, for
K+ channel-associated
protein), which modulates the expression of Kv2 channels
in heterologous expression system assays. KChAP interacts with the N
termini of Kv
Cloning and Expression of a Novel K+ Channel
Regulatory Protein, KChAP
, Department of Biochemistry, and the ¶ Department of
Physiology and Biophysics, Case Western Reserve University,
Cleveland, Ohio 44109-1998
2 subunits, as well as the N termini of Kv1 and the
C termini of Kv
subunits. Kv2.1 and KChAP were coimmunoprecipitated
from in vitro translation reactions supporting a direct
interaction between the two proteins. The amplitudes of Kv2.1 and Kv2.2
currents are enhanced dramatically in Xenopus oocytes
coexpressing KChAP, but channel kinetics and gating are unaffected.
Although KChAP binds to Kv1.5, it has no effect on Kv1.5 currents. We
suggest that KChAP may act as a novel type of chaperone protein to
facilitate the cell surface expression of Kv2 channels.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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