ArticlePflugers Archiv : European journal of physiology2004
The Kv4.2 N-terminal restores fast inactivation and confers KChlP2 modulatory effects on N-terminal-deleted Kv1.4 channels.
Article in Pflugers Archiv : European journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Mechanisms of closed-state inactivation in voltage-gated ion channels.The Journal of physiology · 2011Review
- Dynamic coupling of voltage sensor and gate involved in closed-state inactivation of kv4.2 channels.The Journal of general physiology · 2009Article
- K+ channels in apoptosis.The Journal of membrane biology · 2006Review
- Transient outward potassium current, 'Ito', phenotypes in the mammalian left ventricle: underlying molecular, cellular and biophysical mechanisms.The Journal of physiology · 2005Review
- K(V)4.2 channels tagged in the S1-S2 loop for alpha-bungarotoxin binding provide a new tool for studies of channel expression and localization.Channels (Austin, Tex.)Article
- K(V)4.3 N-terminal deletion mutant Δ2-39: effects on inactivation and recovery characteristics in both the absence and presence of KChIP2b.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal end of the subunits of the voltage-gated K+ channel Kv1.4 is essential for their rapid N-type inactivation, but removal of the entire Kv4.2 N-terminus slows inactivation only moderately. In this study, we investigated the effect of substituting the Kv4.2 N-terminal for that of Kv1.4 subunits. Despite the minor role of the Kv4.2 N-terminal in Kv4.2 inactivation and the limited degree of amino acid identity between Kv1.4 and Kv4.2 N-terminals, attachment of the Kv4.2 N-terminal to inactivation-deficient, N-terminal-deleted Kv1.4 subunits restored rapid inactivation. The Kv4.2 N-terminal/N-deleted Kv1.4 chimeric construct had inactivation kinetics like those of Kv4.2, inactivation voltage-dependence resembling Kv1.4 and recovery from inactivation substantially faster than wild-type Kv1.4. Acceleration of reactivation appeared to be due to the ability of chimeric channels to recover from inactivation without passing through the open state. Co-expression of wild-type Kv1.4 with the K+ channel interacting protein-2 (KChIP2) did not alter Kvl.4 properties, but co-expression of KChIP2 with Kv4.2 N-terminal/N-deleted Kv1.4 chimeric subunits significantly increased current expression and slowed inactivation without altering the rate of recovery from inactivation. We conclude that substitution of the Kv4.2 N-terminal for that of Kv1.4 transfers a variety of properties of Kv4.2, including inactivation time-dependence, accelerated recovery from inactivation and interaction with KChIP2, to Kv1.4, indicating the ability of Kvl.4 subunits to display these properties and the sufficiency of the Kv4.2 N-terminal to convey them.
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