Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 7(88), p. 2931-2935, 1991

DOI: 10.1073/pnas.88.7.2931

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 1991 by Ken McCormack, Mark A. Tanouye, Linda E. Iverson, Jen-Wei Lin, Mani Ramaswami, Tom McCormack, James T. Campanelli, Mathew K. Mathew ORCID, Bernardo Rudy
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Green circle
Postprint: archiving allowed
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

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.