A component of calcium-activated potassium channels encoded by the Drosophila slo locus
- PMID: 1857984
- DOI: 10.1126/science.1857984
A component of calcium-activated potassium channels encoded by the Drosophila slo locus
Abstract
Calcium-activated potassium channels mediate many biologically important functions in electrically excitable cells. Despite recent progress in the molecular analysis of voltage-activated K+ channels, Ca(2+)-activated K+ channels have not been similarly characterized. The Drosophila slowpoke (slo) locus, mutations of which specifically abolish a Ca(2+)-activated K+ current in muscles and neurons, provides an opportunity for molecular characterization of these channels. Genomic and complementary DNA clones from the slo locus were isolated and sequenced. The polypeptide predicted by slo is similar to voltage-activated K+ channel polypeptides in discrete domains known to be essential for function. Thus, these results indicate that slo encodes a structural component of Ca(2+)-activated K+ channels.
Similar articles
-
A distinct potassium channel polypeptide encoded by the Drosophila eag locus.Science. 1991 Jun 14;252(5012):1560-2. doi: 10.1126/science.1840699. Science. 1991. PMID: 1840699
-
Complementation of physiological and behavioral defects by a slowpoke Ca(2+) -activated K(+) channel transgene.J Neurochem. 2000 Sep;75(3):1310-9. doi: 10.1046/j.1471-4159.2000.751310.x. J Neurochem. 2000. PMID: 10936215
-
Identification and characterization of a putative C. elegans potassium channel gene (Ce-slo-2) distantly related to Ca(2+)-activated K(+) channels.Gene. 1999 Nov 15;240(1):35-43. doi: 10.1016/s0378-1119(99)00398-4. Gene. 1999. PMID: 10564810
-
Behavioral and electrophysiological analysis of Ca-activated K-channel transgenes in Drosophila.Ann N Y Acad Sci. 1998 Nov 16;860:296-305. doi: 10.1111/j.1749-6632.1998.tb09057.x. Ann N Y Acad Sci. 1998. PMID: 9928320 Review.
-
The molecular biology of K+ channels.Curr Opin Cell Biol. 1991 Aug;3(4):663-70. doi: 10.1016/0955-0674(91)90039-2. Curr Opin Cell Biol. 1991. PMID: 1772658 Review.
Cited by
-
An extracellular domain of the accessory β1 subunit is required for modulating BK channel voltage sensor and gate.J Gen Physiol. 2012 Jan;139(1):57-67. doi: 10.1085/jgp.201110698. Epub 2011 Dec 12. J Gen Physiol. 2012. PMID: 22155735 Free PMC article.
-
Interactions between β-catenin and the HSlo potassium channel regulates HSlo surface expression.PLoS One. 2011;6(12):e28264. doi: 10.1371/journal.pone.0028264. Epub 2011 Dec 14. PLoS One. 2011. PMID: 22194818 Free PMC article.
-
Molecular mechanism of pharmacological activation of BK channels.Proc Natl Acad Sci U S A. 2012 Feb 28;109(9):3552-7. doi: 10.1073/pnas.1114321109. Epub 2012 Feb 13. Proc Natl Acad Sci U S A. 2012. PMID: 22331907 Free PMC article.
-
BK-type calcium-activated potassium channels: coupling of metal ions and voltage sensing.J Physiol. 2010 Dec 1;588(Pt 23):4651-8. doi: 10.1113/jphysiol.2010.194514. Epub 2010 Jul 26. J Physiol. 2010. PMID: 20660558 Free PMC article. Review.
-
Role of the beta1 subunit in large-conductance Ca(2+)-activated K(+) channel gating energetics. Mechanisms of enhanced Ca(2+) sensitivity.J Gen Physiol. 2000 Sep;116(3):411-32. doi: 10.1085/jgp.116.3.411. J Gen Physiol. 2000. PMID: 10962017 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous