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Journal of Neuroscience, Vol 10, 2903-2916, Copyright © 1990 by Society for Neuroscience
The role of the divergent amino and carboxyl domains on the inactivation properties of potassium channels derived from the Shaker gene of Drosophila
LE Iverson and B Rudy
Division of Neurosciences, Beckman Research Institute of the City of Hope, Duarte, California 91010.
Several products generated from the Drosophila Shaker gene by alternative
splicing predict a group of similar proteins with an identical central and
variable amino and carboxyl domains. We have constructed 9 Sh cDNAs
combining 3 different 5' domains with 3 different 3' domains. RNA
transcribed from 6 of these cDNAs induce K+ currents in Xenopus oocytes.
All currents share similar properties of voltage dependence, potassium
selectivity, and block by 4-AP, TEA, and charybdotoxin. These properties
presumably result from a channel core formed by the identical central
region of the proteins. The currents differ in macroscopic inactivation
kinetics. Five RNAs induced K+ currents which inactivate, each at distinct
rates, during short depolarizations. The sixth RNA induces a current that
essentially does not inactivate unless depolarized for many seconds. This
raises the possibility that Sh may encode nontransient as well as transient
K+ currents. Analysis of currents produced by the various combinations
suggests that the divergent amino domains influence the stability of a
first, nonabsorbing, inactivated state. This results in striking
differences in the probability of channel reopening, as observed in
single-channel recordings, of those channels with identical carboxyl but
different amino domains. Furthermore, based on macroscopic analysis of the
currents, we suggest that the primary role of the carboxyl domains is to
influence the relative stability between the first and a second inactivated
state. The second inactivated state is essentially absorbing, and recovery
from this state is very slow. The observed differences in the rates of
recovery from inactivation of channels containing different carboxyl
domains reflect differences in the rates at which they enter this second
inactivated state.
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