Block of Shaker potassium channels by external calcium ions.
We describe an interaction between external Ca(2+) ions and Shaker K channels that is important in the gating of the channels. The interaction was first detected as a partial block of inward K(+) current in elevated Ca(2+), beginning near -40 mV and becoming stronger at more negative voltage. Surprisingly, the time course of the block can be resolved as a rapid decay of inward current magnitude following a repolarizing step. The rapid decay of current is shown to be the result of channel block by using a two-pulse procedure that monitors the time course of gate closing. As a result of block, the decay of the tail current after repolarization is two to three times faster than gate closing. With physiological values for voltage and calcium concentration, block is readily detectable from tail time course, implying that it occurs as a normal concomitant of gate closing in Shaker. The slight voltage dependence of block from -60 to -100 mV suggests that Ca(2+) is bound (with low affinity) near the outer mouth of the channel. Elevated calcium quickens the inward gating current recorded as Shaker channels are closing; this current approximately doubles in amplitude and has a faster time course and quicker rising phase. When combined, the results suggest that calcium accelerates the first step in closing of the channel gate, perhaps by changing the channel's ion-occupancy state.
Gomez-Lagunas
Froylan
F
School of Medicine, National University of Mexico, Mexico City, 04510, Mexico.
Melishchuk
Alexey
A
Armstrong
Clay M
CM
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D015640:Ion Channel Gating / Q000502:physiology; D007700:Kinetics; D008564:Membrane Potentials / Q000187:drug effects; D015221:Potassium Channels / Q000187:drug effects / Q000502:physiology*; D051637:Shaker Superfamily of Potassium Channels; D018411:Spodoptera; D014162:Transfection
D015221:Potassium Channels; D051637:Shaker Superfamily of Potassium Channels; D002118:Calcium