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Biophys J, February 2002, p. 781-792, Vol. 82, No. 2
Laboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706 USA
TOK1 encodes the channel
responsible for the prominent outward K+ current of the
yeast plasma membrane. It can dwell in several impermeable states,
including a rapidly transiting,
K+-electromotive-force-dependent "R"
(rectifying) state, a voltage-independent "IB"
(interburst) state, and a set of
[K+]ext and voltage-dependent "C"
(closed) states. Whereas evidence suggests that the C
states result from the constriction of an inner gate at the cytosolic
end of the pore, R is most likely an intrinsic gating property of the
K+ filter. Here, we present evidence that Tok1's
carboxyl-tail domain also plays an intimate role in channel gating by
dynamically preventing inner-gate closures. We present an integrated
model of TOK1 gating in which the filter gate, inner gate, and carboxyl
tail interact to produce the various phenomenological states. Both
wild-type and tailless behaviors can be replicated using Monte Carlo
computer simulations based on this model.
Biophys J, February 2002, p. 781-792, Vol. 82, No. 2
© 2002 by the Biophysical Society 0006-3495/02/02/781/12 $2.00
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