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  N-Terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability

Höllerer-Beitz, G., Schönherr, R., Koenen, M., & Heinemann, S. H. (1999). N-Terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability. Pflügers Archiv: European Journal of Physiology, 438(2), 141-146. doi:10.1007/s004240050891.

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Genre: Journal Article
Alternative Title : N-Terminal deletions of rKv1.4 channels affect the voltage dependence of channel availability

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PflügArch_438_1999_141.pdf (Any fulltext), 66KB
 
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Höllerer-Beitz, Gerhild, Author
Schönherr, Roland, Author
Koenen, Michael1, 2, Author              
Heinemann, Stefan H., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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Free keywords: Activation; Inactivation; Mutagenesi; Potassium channels
 Abstract: Rat Kv1.4 potassium channels undergo rapid inactivation, which is mediated by the N-terminal structure of the polypeptide. This inactivation can be removed by N-terminal deletion of about 20 residues. However, more substantial deletion (e.g. 37 residues) restores inactivation suggesting a second inactivating domain [Kondoh et al. J Biol Chem 272:19333-19338, 1997]. Here we provide evidence that this inactivation shares all properties with N-type inactivation. Pore mutations, which are supposed to affect C-type inactivation, have no effect. In addition, the redox regulation of inactivation, which is typical for Kv1.4 channels, can be conferred to the inactivation of the deleted constructs by incorporation of an N-terminal cysteine residue. The most remarkable feature of this secondary inactivation is the existence of two components in the steady-state voltage dependence of inactivation. For mutant rKv1.42-37 about 90% of the channels only activate when the holding membrane potential is more negative than about -120 mV; the remaining 10% show the typical threshold at -60 mV. Mutagenesis of the truncated channel affected the relative amplitudes of these two components, but not the voltage dependence. The results suggest that the secondary ball structures of rKv1.4 channels interact with the protein structures responsible for activation

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Language(s): eng - English
 Dates: 1999-02-031999-03-151999-06-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666079
DOI: 10.1007/s004240050891
URI: http://www.ncbi.nlm.nih.gov/pubmed/10370099
Other: 5355
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Title: Pflügers Archiv: European Journal of Physiology
  Other : Pflügers Arch. Europ. J. Physiol.
Source Genre: Journal
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Publ. Info: Heidelberg : Springer-Verlag
Pages: - Volume / Issue: 438 (2) Sequence Number: - Start / End Page: 141 - 146 Identifier: ISSN: 0031-6768
CoNE: https://pure.mpg.de/cone/journals/resource/954925432380