TASK-3, a new member of the tandem pore K(+) channel family
- PMID: 10734076
- DOI: 10.1074/jbc.275.13.9340
TASK-3, a new member of the tandem pore K(+) channel family
Abstract
We have isolated from the rat cerebellum cDNA library a complementary DNA encoding a new member of the tandem pore K(+) channel family. Its amino acid sequence shares 54% identity with that of TASK-1, but less than 30% with those of TASK-2 and other tandem pore K(+) channels (TWIK, TREK, TRAAK). Therefore, the new clone was named TASK-3. Reverse transcriptase-polymerase chain reaction analysis showed that TASK-3 mRNA is expressed in many rat tissues including brain, kidney, liver, lung, colon, stomach, spleen, testis, and skeletal muscle, and at very low levels in the heart and small intestine. When expressed in COS-7 cells, TASK-3 exhibited a time-independent, noninactivating K(+)-selective current. Single-channel conductance was 27 pS at -60 mV and 17 pS at 60 mV in symmetrical 140 mM KCl. TASK-3 current was highly sensitive to changes in extracellular pH (pH(o)), a hallmark of the TASK family of K(+) channels. Thus, a change in pH(o) from 7.2 to 6.4 and 6.0 decreased TASK-3 current by 74 and 96%, respectively. Mutation of histidine at position 98 to aspartate abolished pH(o) sensitivity. TASK-3 was blocked by barium (57%, 3 mM), quinidine (37%, 100 microM), and lidocaine (62%, 1 mM). Thus, TASK-3 is a new member of the acid-sensing K(+) channel subfamily (TASK).
Similar articles
-
TREK-2, a new member of the mechanosensitive tandem-pore K+ channel family.J Biol Chem. 2000 Jun 9;275(23):17412-9. doi: 10.1074/jbc.M000445200. J Biol Chem. 2000. PMID: 10747911
-
TASK-3, a novel tandem pore domain acid-sensitive K+ channel. An extracellular histiding as pH sensor.J Biol Chem. 2000 Jun 2;275(22):16650-7. doi: 10.1074/jbc.M000030200. J Biol Chem. 2000. PMID: 10747866
-
Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family.J Biol Chem. 2004 Jul 2;279(27):28063-70. doi: 10.1074/jbc.M402940200. Epub 2004 Apr 27. J Biol Chem. 2004. PMID: 15123670
-
Molecular and functional properties of two-pore-domain potassium channels.Am J Physiol Renal Physiol. 2000 Nov;279(5):F793-801. doi: 10.1152/ajprenal.2000.279.5.F793. Am J Physiol Renal Physiol. 2000. PMID: 11053038 Review.
-
K+ conductance activated during regulatory volume decrease. The channels in Ehrlich cells and their possible molecular counterpart.Comp Biochem Physiol A Mol Integr Physiol. 2001 Oct;130(3):565-75. doi: 10.1016/s1095-6433(01)00428-7. Comp Biochem Physiol A Mol Integr Physiol. 2001. PMID: 11913467 Review.
Cited by
-
TASK channels in arterial chemoreceptors and their role in oxygen and acid sensing.Pflugers Arch. 2015 May;467(5):1013-25. doi: 10.1007/s00424-015-1689-1. Epub 2015 Jan 28. Pflugers Arch. 2015. PMID: 25623783 Free PMC article. Review.
-
Major channels involved in neuropsychiatric disorders and therapeutic perspectives.Front Genet. 2013 May 7;4:76. doi: 10.3389/fgene.2013.00076. eCollection 2013. Front Genet. 2013. PMID: 23675382 Free PMC article.
-
TASK-like conductances are present within hippocampal CA1 stratum oriens interneuron subpopulations.J Neurosci. 2006 Jul 12;26(28):7362-7. doi: 10.1523/JNEUROSCI.1257-06.2006. J Neurosci. 2006. PMID: 16837582 Free PMC article.
-
Neutralization of a single arginine residue gates open a two-pore domain, alkali-activated K+ channel.Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):666-71. doi: 10.1073/pnas.0606173104. Epub 2006 Dec 29. Proc Natl Acad Sci U S A. 2007. PMID: 17197424 Free PMC article.
-
Carotid body chemosensory responses in mice deficient of TASK channels.J Gen Physiol. 2010 Apr;135(4):379-92. doi: 10.1085/jgp.200910302. J Gen Physiol. 2010. PMID: 20351062 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
