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1.2 interactions and their
effects on cardiac Kv channel expression
1 The Rammelkamp Center for Education and Research, MetroHealth Campus, and Departments of 2 Physiology and Biophysics and 3 Biochemistry, Case Western Reserve University, Cleveland, Ohio 44109
KChAP and voltage-dependent K+ (Kv)
-subunits are two different types of cytoplasmic proteins that
interact with Kv channels. KChAP acts as a chaperone for Kv2.1 and
Kv4.3 channels. It also binds to Kv1.x channels but, with the exception
of Kv1.3, does not increase Kv1.x currents. Kv-subunits are
assembled with Kv1.x channels; they exhibit "chaperone-like"
behavior and change gating properties. In addition, KChAP and
Kv-subunits interact with each other. Here we examine the
consequences of this interaction on Kv currents in Xenopus
oocytes injected with different combinations of cRNAs, including
Kv1.2, KChAP, and either Kv1.4, Kv1.5, Kv2.1, or Kv4.3. We found
that KChAP attenuated the depression of Kv1.5 currents produced by
Kv1.2, and Kv1.2 eliminated the increase of Kv2.1 and Kv4.3
currents produced by KChAP. Both KChAP and Kv1.2 are expressed in
cardiomyocytes, where Kv1.5 and Kv2.1 produce sustained outward
currents and Kv4.3 and Kv1.4 generate transient outward currents.
Because they interact, either KChAP or Kv1.2 may alter both
sustained and transient cardiac Kv currents. The interaction of these
two different classes of modulatory proteins may constitute a novel
mechanism for regulating cardiac K+ currents.
chaperone; modulation; potassium channels; voltage-gated potassium 1.4 channel; voltage-gated potassium 1.5 channel; voltage-gated potassium 2.1 channel; voltage-gated potassium 4.3 channel
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