UNSPECIFIED. (2001) TASK-5, a novel member of the tandem pore K+ channel family. PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 442 (6). pp. 828-833. ISSN 0031-6768

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Abstract

We have cloned a novel member of the tandem pore K+ channel family from human brain cDNA. The novel cDNA encodes a 330-residue polypeptide of predicted molecular mass 36 kDa. We have named the channel TASK-5 owing to its sequence homology with TASK-1 and TASK-3. TASK-5 mRNA is expressed in pancreas, liver, kidney. lung, ovary, testis and heart. However, expression of TASK-5 in heterologous systems failed to elicit ionic currents. Removal of a putative endoplasmic reticulum retention sequence did not alter this finding and the distribution of channel proteins in HEK293 cells was similar for both TASK-1 and TASK-5. We tested whether TASK-5 could form heteromers with TASK-1. We show a mutant form of TASK-1 (H98N) to have a radically reduced sensitivity to acidification. Proton sensitivity could be rescued by injecting equimolar amounts of wild-type and mutant TASK-1 cRNA into Xenopus oocytes; the effect was that expected if half the channels formed are heteromers. Co-expression of TASK-5 with TASK-1 H98N does not affect the proton sensitivity of mutant TASK-1: thus TASK-5 appears not to form heteromers with TASK-1. Nonetheless. TASK-5 may require some other, unidentified partner subunit to form functional channels in the plasma membrane or it may form a channel in an intracellular organelle.

Item Type:	Journal Article
Subjects:	Q Science > QP Physiology
Journal or Publication Title:	PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
Publisher:	SPRINGER-VERLAG
ISSN:	0031-6768
Date:	September 2001
Volume:	442
Number:	6
Number of Pages:	6
Page Range:	pp. 828-833
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/11697

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