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          Institute: MPI für biophysikalische Chemie     Collection: Abteilungsunabhängige Arbeitsgruppen     Display Documents



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ID: 233178.0, MPI für biophysikalische Chemie / Abteilungsunabhängige Arbeitsgruppen
Expression pattern in brain of TASK-1, TASK-3, and a tandem pore domain K+ channel subunit, TASK-5, associated with the central auditory nervous system
Authors:Karschin, C.; Wischmeyer, E.; Preisig-Mueller, R.; Rajan, S.; Derst, C.; Grzeschik, K. H.; Daut, J.; Karschin, A.
Language:English
Date of Publication (YYYY-MM-DD):2001-12
Title of Journal:Molecular and Cellular Neuroscience
Volume:18
Issue / Number:6
Start Page:632
End Page:648
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:TWIK-related acid-sensitive K+ (TASK) channels contribute to setting the resting potential of mammalian neurons and have recently been defined as molecular targets for extracellular protons and volatile anesthetics. We have isolated a novel member of this subfamily, hTASK-5, from a human genomic library and mapped it to chromosomal region 20q12-20q13. hTASK-5 did not functionally express in Xenopus oocytes, whereas chimeric TASK-5/TASK-3 constructs containing the region between M1 and M3 of TASK-3 produced K+ selective currents. To better correlate TASK subunits with native K+ currents in neurons the precise cellular distribution of all TASK family members was elucidated in rat brain. A comprehensive in situ hybridization analysis revealed that both TASK-1 and TASK-3 transcripts are most strongly expressed in many neurons likely to be cholinergic, serotonergic, or noradrenergic. In contrast, TASK- 5 expression is found in olfactory bulb mitral cells and Purkinje cells, but predominantly associated with the central auditory pathway. Thus, TASK-5 K+ channels, possibly in conjunction with auxiliary proteins, may play a role in the transmission of temporal information in the auditory system.
Comment of the Author/Creator:Date: 2001, DEC
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/AG Andreas Karschin
External Affiliations:Univ Wurzburg, Inst Physiol, Wurzburg, Germany; Univ Marburg, Inst Physiol, Marburg, Germany; Univ Marburg, Inst Human Genet, Marburg, Germany
Identifiers:URL:http://www.sciencedirect.com/science?_ob=MImg&_ima...
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