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Vol. 285, Issue 3, 1051-1060, June 1998
Neurex Corporation, 3760 Haven Avenue, Menlo Park, California
The ability of voltage-gated potassium channel 
-subunits to form
heteromultimers has complicated efforts to use toxins to characterize
potassium channels in native cells. Here I investigate the effects of
subunit composition on toxin blocking affinity, using three members of
the Shaker subfamily of potassium channel -subunits (Kv1.1, Kv1.2
and Kv1.4), which are known to form heteromultimers in vivo,
in the Xenopus oocyte expression system. These subunits were
coexpressed as pairs in which one member was toxin-sensitive and the
other relatively insensitive. The blocking affinity of two dendrotoxins
(DTX-I and 
-DTX) and a scorpion toxin (tityustoxin-K) on the
resulting mixed population of channels was measured to evaluate three
models of toxin block. The single subunit model, in which a single
toxin-sensitive subunit renders the channel toxin sensitive, best
described all of the data for the two dendrotoxins and the block of
tityustoxin-K for a mixed population of channels composed of Kv1.1
and Kv1.2 subunits. However, with tityustoxin-K, the data for a
mixed population of Kv1.2 and Kv1.4 subunits was fit best by a model in
which the toxin interacts with all four subunits for high-affinity
block. The data suggest that subunit composition of potassium channels
can have a large effect on toxin block and that different toxins yield
strikingly diverse results with the same pair of subunits, even when
they are nearly identical in blocking affinity for the toxin-sensitive
subunit.
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