NDLI: The Kv4.2 N-terminal restores fast inactivation and confers KChIP2 modulatory effects on N-terminal-deleted Kv1.4 channels

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The Kv4.2 N-terminal restores fast inactivation and confers KChIP2 modulatory effects on N-terminal-deleted Kv1.4 channels

Content Provider	Springer Nature Link
Author	Pourrier, Marc Herrera, Daniel Caballero, Ricardo Schram, Gert Wang, Zhiguo Nattel, Stanley
Copyright Year	2004
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 Kv1.4 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 Kv1.4 subunits to display these properties and the sufficiency of the Kv4.2 N-terminal to convey them.
Starting Page	235
Ending Page	247
Page Count	13
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	449
Issue Number	3
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-09-28
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Potassium channels Inactivation Ionic currents Cardiac electrophysiology Beta subunits Alpha subunits Voltage-gated channels
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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The Kv4.2 N-terminal restores fast inactivation and confers KChIP2 modulatory effects on N-terminal-deleted Kv1.4 channels

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