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          Document History for Document ID 16496.0

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Document Version Version Comment Date Status
16496.0 [No comment] 21.09.2010 15:55 Released

ID: 16496.0, MPI für biophysikalische Chemie / Molekulare Entwicklungsbiologie (Prof. Herbert Jäckle)
Inwardly rectifying K+ (Kir) channels in Drosophila - A crucial role of cellular milieu factors for Kir channel function
Authors:Doering, F.; Wischmeyer, E.; Kuehnlein, R. P.; Jaeckle, H.; Karschin, A.
Language:English
Date of Publication (YYYY-MM-DD):2002-07-12
Title of Journal:Journal of Biological Chemistry
Volume:277
Issue / Number:28
Start Page:25554
End Page:25561
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Three cDNAs encoding inwardly rectifying potassium (Kir) channels were isolated from Drosophila melanogaster. The protein sequences of Drosophila KirI (dKirI) and dKirII are moderately (<44%) and dKirIII sequence is weakly (<27%) identical to human Kir channel subunits. During fly development, five dKir channel transcripts derived from three genes are differentially expressed. Whole mount in situ hybridizations revealed dKirI transcripts absent from embryos, but dKirII and dKirIII are expressed in the embryonic hind gut and in Malpighian tubules, respectively, thus covering the entire osmoregulatory system of the developing fly. In the head of adult flies, predominantly dKirII transcripts were detected. When expressed in Xenopus oocytes, dKir channel activity was only observed after amino acid substitutions in their cytosolic tails (e.g. exchange of a unique valine in the NH2 terminus). In contrast, heterologous expression of wild type dKirI and dYirII in Drosophila S2 cells readily evoked typical inwardly rectifying K+ currents, which were weakly sensitive to Ba2+. Thus, the specific milieu of insect cells provides a crucial cellular environment for proper function of dKir channels.
Comment of the Author/Creator:Date: 2002, JUL 12
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Herbert Jäckle / 170
MPI für biophysikalische Chemie/Abt. Erwin Neher / 140
MPI für biophysikalische Chemie/AG Ronald Kühnlein
External Affiliations:Univ Wurzburg, Inst Physiol, D-97070 Wurzburg, Germany
Identifiers:URL:http://www.jbc.org/content/277/28/25554.full.pdf+h...