Abstract
Kv4.3 encodes the pore-forming subunit of the cardiac transient outward potassium current (Ito). hKv4.3-encoded current does not fully replicate cardiac Ito, suggesting a functionally significant role for accessory subunits. KChIP2 associates with Kv4.3 and modifies hKv4.3-encoded currents but does not replicate native Ito. We examined the effect of several ancillary subunits expressed in the heart on hKv4.3-encoded currents. Remarkably, the ancillary subunits Kvβ3, minK, MiRP-1, the Na channel β1 and KChIP2 increased the density and modified the gating of hKv4.3 current. hKv4.3 promiscuously assembles with ancillary subunits in vitro, functionally modifying the encoded currents; however, the physiological significance is uncertain.
Original language | English (US) |
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Pages (from-to) | 183-188 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 528 |
Issue number | 1-3 |
DOIs | |
State | Published - Sep 25 2002 |
Keywords
- Accessory subunit
- Ion channel
- Potassium
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology