Abstract
Kcv is a K+-selective channel encoded by the Paramecium bursaria Chlorella virus 1 (PBVC-1). Expression of this protein, so far the smallest known functional K+ channel, in Xenopus oocytes reveals an instantaneous and a time-dependent component during voltage-clamp steps. These two components have an identical sensitivity to the inhibitor amantadine, implying that they reflect distinct kinetic features of the same channel. About 70% of the channels are always open; at hyperpolarizing voltages the time-dependent channels (30%) open in a voltage-dependent manner reaching half-maximal activation at about -70 mV. At both extreme positive and negative voltages the open-channel conductance decreases in a voltage-dependent manner. To examine the mechanism underlying the voltage-dependence of Kcv we neutralized the two charged amino acids in the lipophilic N-terminus. However, this double mutation had no effect on the voltage-dependence of the channel, ruling against the possibility that these charged amino acids represent a membrane-embedded voltage sensor. We have considered whether a block by external divalent cations is involved in the voltage-dependence of the channel. The Kcv current was increased about 4-fold on reduction of external Ca2+ concentration by a factor of ten. This pronounced increase in current was observed on lowering Ca2+ but not Mg2+ and was voltage-independent. These data indicate a Ca2+-selective, but voltage-independent mechanism for regulation of channel conductance.
Original language | English (US) |
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Pages (from-to) | 15-25 |
Number of pages | 11 |
Journal | Journal of Membrane Biology |
Volume | 187 |
Issue number | 1 |
DOIs | |
State | Published - May 1 2002 |
Keywords
- Ca block
- K channel
- Kcv
- PBCV-1
- Voltage-dependence
ASJC Scopus subject areas
- Biophysics
- Physiology
- Cell Biology