Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 3629K) PDF+supp data (5926K) PPT slides of all figures Supplemental Material Index Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JGP Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Labro, A. J. Articles by Snyders, D. J. Search for Related Content PubMed PubMed Citation Articles by Labro, A. J. Articles by Snyders, D. J. Pubmed/NCBI databases Gene GEO Profiles HomoloGene Protein UniGene Social Bookmarking                            What's this?

¹ Laboratory for Molecular Biophysics, Physiology, and Pharmacology, Department of Biomedical Sciences, University of Antwerp, 2610 Antwerp, Belgium
² Consorzio Interuniversitario per le Applicazioni del Supercalcolo per Universita e Ricerca (CASPUR), 00185 Rome, Italy
³ Laboratory for Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford OX1 4BH, England, UK

Correspondence to Dirk J. Snyders: dirk.snyders{at}ua.ac.be

Voltage-dependent K⁺ channels transfer the voltage sensor movement into gate opening or closure through an electromechanical coupling. To test functionally whether an interaction between the S4-S5 linker (L45) and the cytoplasmic end of S6 (S6_T) constitutes this coupling, the L45 in hKv1.5 was replaced by corresponding hKv2.1 sequence. This exchange was not tolerated but could be rescued by also swapping S6_T. Exchanging both L45 and S6_T transferred hKv2.1 kinetics to an hKv1.5 background while preserving the voltage dependence. A one-by-one residue substitution scan of L45 and S6_T in hKv1.5 further shows that S6_T needs to be -helical and forms a "crevice" in which residues I422 and T426 of L45 reside. These residues transfer the mechanical energy onto the S6_T crevice, whereas other residues in S6_T and L45 that are not involved in the interaction maintain the correct structure of the coupling.

© 2008 Labro et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				S. K. Upadhyay, P. Nagarajan, and M. K. Mathew Potassium channel opening: a subtle two-step J. Physiol., August 1, 2009; 587(15): 3851 - 3868. [Abstract] [Full Text] [PDF]

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents