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PMID: 2011602 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 7 ·1991-04-01 ·Pages 2931-5

McCormack K, Tanouye MA, Iverson LE, Lin JW, Ramaswami M, McCormack T, Campanelli JT, Mathew MK, Rudy B

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.

Related Genes

MeSH Terms

Amino Acid Sequence Animals Cell Membrane/physiology Drosophila/genetics Female Humans Ion Channel Gating Leucine Membrane Potentials Models, Molecular Molecular Sequence Data Mutagenesis Oocytes/physiology Potassium Channels/genetics,physiology Protein Conformation Sequence Homology, Nucleic Acid Transcription, Genetic Xenopus

Chemicals

Potassium Channels Leucine

Authors & Affiliations

9 authors, click to expand affiliations / ORCID

McCormack K

Division of Biology 216-76, California Institute of Technology, Pasadena 91125.

Tanouye M A

Iverson L E

Lin J W

Ramaswami M

McCormack T

Campanelli J T

Mathew M K

Rudy B

References (24)

24 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.88.7.2931

Published

1991-04-01

Pages

2931-5

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC51354

Subset

Grants

NIGMS NIH HHS · GM26976 · United States

NIGMS NIH HHS · GM42824 · United States

NINDS NIH HHS · NS21327 · United States

External Links

PubMed source DOI: 10.1073/pnas.88.7.2931 PMC Full Text View journal details

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

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