ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Transplanting the n-terminus from Kv1.4 to Kv1.1 generates an inwardly rectifying K+ channel

Chanda, B and Tiwari, JK and Varshney, A and Mathew, MK (1999) Transplanting the n-terminus from Kv1.4 to Kv1.1 generates an inwardly rectifying K+ channel. In: NeuroReport, 10 (2). pp. 237-241.

Full text not available from this repository. (Request a copy)
Official URL: http://journals.lww.com/neuroreport/Abstract/1999/...

Abstract

A chimeric channel, 4N/1, was generated from two outwardly rectifying K+ channels by linking the N-terminal cytoplasmic domain of hKv1.4 (N terminus ball and chain of hKv1.4) with the transmembrane body of hKvl.l (Delta 78N1 construct of hKvl.l). The recombinant channel has properties similar to the six transmembrane inward rectifiers and opens on hyperpolarization with a threshold of activation at -90 mV. Outward currents are seen on depolarization provided the channel is first exposed to a hyperpolarizing pulse of -100mV or more. Hyperpolarization at and beyond -130mV provides evidence of channel deactivation. Delta 78N1 does not show inward currents on hyperpolarization but does open on depolarizing from -80mV with characteristics similar to native hKvl.l. The outward currents seen in both Delta 78N1 and 4N/1 inactivate slowly at rates consistent with C-type inactivation. The inward rectification of the 4N/1 chimera is consistent with the inactivation gating mechanism. This implies that the addition of the N-terminus from hKv1.4 to hKvl.l shifts channel activation to hyperpolarizing potentials. These results suggest a mechanism involving the N-terminal cytoplasmic domain for conversion of outward rectifiers to inward rectifiers. (C) 1999 Lippincott Williams & Wilkins.

Item Type: Journal Article
Publication: NeuroReport
Publisher: Lippincott Williams and Wilkins
Additional Information: Copyright of this article belongs to Lippincott Williams and Wilkins.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 03 Aug 2011 07:05
Last Modified: 12 Oct 2018 14:17
URI: http://eprints.iisc.ac.in/id/eprint/38904

Actions (login required)

View Item View Item