The Library
TASK-5, a novel member of the tandem pore K+ channel family
Tools
Tools
Tools
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
Full text not available from this repository.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 | ||||
| Official Date: | September 2001 | ||||
| Dates: |
|
||||
| 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 |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Actions (login required)
 |
View Item |
