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September 1, 1995Biophysical Journal164 citationsOpen Access

C-type inactivation of a voltage-gated K+ channel occurs by a cooperative mechanism

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GPGyörgy PanyiZSZ ShengCDCarol Deutsch

Key Result

The A413V mutation in the Kv1.3 channel decreased the median inactivation time constant to 4 ms compared to 204 ms for the wild-type channel, supporting a cooperative mechanism of C-type inactivation.

Structured PICO

P
Population
Mammalian lymphoid expression system expressing wild-type and mutant (A413V) lymphocyte voltage-gated K+ channel, Kv1.3
I
Intervention
Expression of mutant (A413V) Kv1.3 channels (homo- and heteromultimeric)
C
Comparator
Wild-type Kv1.3 channels
O
Outcome
Inactivation time constants and kineticssurrogate

C-type inactivation of the Kv1.3 channel occurs via a cooperative mechanism where each subunit contributes equally to the activation free energy.

Main Result

Absolute Event Rate: 4% vs 204%

Abstract

The lymphocyte voltage-gated K+ channel, Kv1.3, inactivates by a C-type process. We have elucidated the molecular basis for this process using a kinetic analysis of wild-type and mutant (A413V) Kv1.3 homo- and heteromultimeric currents in a mammalian lymphoid expression system. The medians of the measured inactivation time constants for wild-type and A413V homotetrameric currents are 204 and 4 ms, respectively. Co-expression of these subunits produces heteromultimeric channels manifesting inactivation kinetics intermediate between those of wild-type and A413V homomultimers. We have considered several models in which each subunit acts either independently or cooperatively to produce the observed inactivation kinetics. The cooperative model gives excellent fits to the data for any heteromultimeric composition of subunits, clearly distinguishing it from the independent models. In the cooperative model, the difference in free energy between the open and inactivated states of the channel is invariant with subunit composition and equals approximately 1.5 kcal/mol. Each subunit contributes equally to the activation free energy for transitions between open and inactivated states, with an A413V subunit decreasing the free energy barrier for inactivation (and for recovery from inactivation) by approximately 0.6 kcal/mol. Our results are consistent with a physical model in which the outer mouth of the channel constricts during C-type inactivation (G. Yellen, D. Sodickson, T. Chen, and M.E. Jurman, 1994, Biophys. J. 66:1068-1075).

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Cite This Study

Panyi et al. (1995) studied Voltage-gated K+ channel (Kv1.3) biophysics. A413V mutation in Kv1.3 channel vs. Wild-type Kv1.3 channel was evaluated on Inactivation time constants. The A413V mutation in the Kv1.3 channel decreased the median inactivation time constant to 4 ms compared to 204 ms for the wild-type channel, supporting a cooperative mechanism of C-type inactivation.

synapsesocial.com/papers/6aa2db19e7c447fa74a8a18ehttps://doi.org/10.1016/s0006-3495(95)79963-5
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