help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Scholle, A.
Right arrow Articles by Benndorf, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Scholle, A.
Right arrow Articles by Benndorf, K.
Biophysical Journal 87:873-882 (2004)
© 2004 The Biophysical Society

Effects of Kv1.2 Intracellular Regions on Activation of Kv2.1 Channels

Annette Scholle *, Thomas Zimmer *, Rolf Koopmann *, Birgit Engeland {dagger}, Olaf Pongs {dagger} and Klaus Benndorf *

* Institut für Physiologie II, Friedrich-Schiller-Universität, 07740 Jena, Germany; and {dagger} Zentrum für Molekulare Neurobiologie, Institut für Neurale Signalverarbeitung, UKE Hamburg, 20251 Hamburg, Germany

Correspondence: Address reprint requests to Dr. Klaus Benndorf, Institut für Physiologie II, Friedrich-Schiller-Universität Jena, D-07740 Jena, Germany. Tel.: 49-3641-934351; Fax: 49-3641-933202; E-mail: klaus.Benndorf{at}mti.uni-jena.de.

Depolarizing voltage steps activate voltage-dependent K+ (Kv) channels by moving the voltage sensor, which triggers a coupling reaction leading to the opening of the pore. We constructed chimeric channels in which intracellular regions of slowly activating Kv2.1 channels were replaced by respective regions of rapidly activating Kv1.2 channels. Substitution of either the N-terminus, S4–S5 linker, or C-terminus generated chimeric Kv2.1/1.2 channels with a paradoxically slow and approximately exponential activation time course consisting of a fast and a slow component. Using combined chimeras, each of these Kv1.2 regions further slowed activation at the voltage of 0 mV, irrespective of the nature of the other two regions, whereas at the voltage of 40 mV both slowing and accelerating effects were observed. These results suggest voltage-dependent interactions of the three intracellular regions. This observation was quantified by double-mutant cycle analysis. It is concluded that interactions between N-terminus, S4–S5 linker, and/or C-terminus modulate the activation time course of Kv2.1 channels and that part of these interactions is voltage dependent.




This article has been cited by other articles:


Home page
J. Neurosci.Home page
D. P. Mohapatra, D. F. Siino, and J. S. Trimmer
Interdomain Cytoplasmic Interactions Govern the Intracellular Trafficking, Gating, and Modulation of the Kv2.1 Channel
J. Neurosci., May 7, 2008; 28(19): 4982 - 4994.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
B. Adair, R. Nunn, S. Lewis, I. Dukes, L. Philipson, and M. Yeager
Single Particle Image Reconstruction of the Human Recombinant Kv2.1 Channel
Biophys. J., March 15, 2008; 94(6): 2106 - 2114.
[Abstract] [Full Text] [PDF]


Home page
J. Neurosci.Home page
M. Xu, R. Cao, R. Xiao, M. X. Zhu, and C. Gu
The Axon Dendrite Targeting of Kv3 (Shaw) Channels Is Determined by a Targeting Motif That Associates with the T1 Domain and Ankyrin G
J. Neurosci., December 19, 2007; 27(51): 14158 - 14170.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Kobrinsky, L. Stevens, Y. Kazmi, D. Wray, and N. M. Soldatov
Molecular Rearrangements of the Kv2.1 Potassium Channel Termini Associated with Voltage Gating
J. Biol. Chem., July 14, 2006; 281(28): 19233 - 19240.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2004 by the Biophysical Society.