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

McCormack, Ken and Tanouye, Mark A. and Iverson, Linda E. and Lin, Jen-Wei and Ramaswami, Mani and McCormack, Tom and Campanelli, James T. and Mathew, Mathew K. and Rudy, Bernardo (1991) 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, 88 (7). pp. 2931-2935. ISSN 0027-8424. https://resolver.caltech.edu/CaltechAUTHORS:20141217-093915812

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.88.7.2931DOIArticle
http://www.pnas.org/content/88/7/2931.abstractPublisherArticle
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.
Funders:
Funding AgencyGrant Number
U.S. Public Health ServiceNS21327
U.S. Public Health ServiceGM42824
U.S. Public Health ServiceGM26976
U.S. Public Health ServiceNS28135
U.S. Public Health ServiceGM29836
Issue or Number:7
Record Number:CaltechAUTHORS:20141217-093915812
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141217-093915812
Official Citation:A role for hydrophobic residues in the voltage-dependent gating of Shaker K+ channels. K McCormack, M A Tanouye, L E Iverson, J W Lin, M Ramaswami, T McCormack, J T Campanelli, M K Mathew, and B Rudy PNAS 1991 88 (7) 2931-2935; doi:10.1073/pnas.88.7.2931
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52942
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:17 Dec 2014 18:01
Last Modified:03 Oct 2019 07:45

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