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Published April 1, 1991 | Published
Journal Article Open

A role for hydrophobic residues in the voltage-dependent gating of Shaker K^+ channels


A leucine heptad repeat is well conserved in voltage-dependent ion channels. Herein we examine the role of the repeat region in Shaker K^+ channels through substitution of the leucines in the repeat and through coexpression of normal and truncated products. In contrast to leucine-zipper DNA-binding proteins, we find that the subunit assembly of Shaker does not depend on the leucine heptad repeat. Instead, we report that substitutions of the leucines in the repeat produce large effects on the observed voltage dependence of conductance voltage and prepulse inactivation curves. Our results suggest that the leucines mediate interactions that play an important role in the transduction of charge movement into channel opening and closing.

Additional Information

© 1991 National Academy of Sciences. Communicated by Norman Davidson, January 7, 1991. We thank H. A. Lester, N. Davidson, X. C. Yang, and R. Dunn for kindly providing rat Ila Na channel RNA; and H. A. Lester for oocytes; D. Rees and T. Kouzarides for helpful discussions; W. N. Zagotta and R. Aldrich for providing a manuscript prior to publication; and R. McMahon for expert technical assistance. This research was supported by U.S. Public Health Service Grants NS21327 and GM42824 to M.A.T., GM26976 to B.R., NS28135 to L.E.I., and GM29836 to H. A. Lester.

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Published - PNAS-1991-McCormack-2931-5.pdf


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