Two cDNAs coding for histamine-gated ion channels in D. melanogaster (original) (raw)

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Accessions

GenBank/EMBL/DDBJ

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Acknowledgements

We thank S. Wagner, A. Stoeck, T. Sobik, M. Bathen and R. Kolarow for technical assistance, and B. Ache and K.F. Störtkuhl for comments on the manuscript.

Author information

Authors and Affiliations

  1. Lehrstuhl für Zellphysiologie, Ruhr-Universität Bochum, Universitätsstraße 150, Bochum, D-44780, Germany
    Günter Gisselmann, Hermann Pusch & Hanns Hatt
  2. AG Molekulare Zellbiochemie, Ruhr-Universität Bochum, Universitätsstraße 150, Bochum, D-44780, Germany
    Bernd T. Hovemann

Authors

  1. Günter Gisselmann
  2. Hermann Pusch
  3. Bernd T. Hovemann
  4. Hanns Hatt

Corresponding author

Correspondence toGünter Gisselmann.

Supplementary information

Supplementary Figure 1.Amino acid alignment.

(a)Tree structure of putative ligand-gated ion channel proteins predicted by the data of the genome sequencing project (all accession numbers beginning with AAF) and already known channel proteins (Rdl: M69057, LCCH3: S62717, Grd: X78349, GluCl: AF297500). The tree was constructed by the program megalign of the Lasergene program package. (JPG 40 kb)

(b)

Amino-acid alignment with DM-HisCl-α1 (AF435469), DM-HisCl-α2 (AF435470), GABA receptor Rdl (M69057), glutamate receptor GluCl (AF297500), the C. elegans serotonin receptor MOD-1 (AF303088) and the murine glycine receptor α1 subunit (C49970). The putative DM-HisCl-α1 protein contains hydrophobic N-terminal residues with sequences highly predictive of a signal cleavage site (http:\\www.cbs.dtu.dk/services/SignalP) which would result in a mature protein beginning at amino-acid residue 22.The putative signal cleavage site in the DM-HisCl-α2 polypeptide is located at pos. 23 and 24. The DM-HisCl-α proteins contain consensus sites for protein kinase C and casein kinase II located between M3 and M4 as well as N-linked glycosylation sites in the proposed extracellular domain (http:\\www.expasy.ch/prosite/). The conserved motifs characteristic of the 'cys-brigde' family of channels, such as a large N-terminal extracellular domain and four hydrophobic transmembrane domains M1-M4, also occur in DM-HisCl-α. The main difference between DM-HisCl-α1 and DM-HisCl-α2 is the large intracellular loop between M3 and M4, which is considerably shorter in DM-HisCl-α2. The protein alignment shows that the DM-HisCl-α proteins are related to Drosophila glutamate- and GABA-gated chloride channels. Similarity to the Drosophila GABA- or glutamate-gated chloride channels Rdl {4942} and GluCl {1677} ranges from 19 to 27% of identical amino acids. Labels above the lines: putative signal sequence, M1-M4 regions, Cys-Cys bridge; ♦ N-glycosylation, ▪ PKC. (PDF 25 kb)

(c)

Alignment of the M2 regions of DM-HisCl-α1/-α2 with the ligand-gated chloride channels Rdl, GluCl, MOD-1 and Gly-alpha1 and the serotonin- and acetylcholine-gated cation channels GP-5HT3As (AF006462) and rat-nAChRαM (X03986). The putative pore-forming M2 regions of HisCl-α are more similar to the M2 regions of other ligand-gated chloride channels from Drosophlia, such as Rdl and GluCl, than to those of ligand-gated cation channels, suggesting that the DM-HisCl-α pore may also be chloride-selective. (PDF 10 kb)

Detailed Figure Legends (PDF 19 kb)

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Gisselmann, G., Pusch, H., Hovemann, B. et al. Two cDNAs coding for histamine-gated ion channels in D. melanogaster.Nat Neurosci 5, 11–12 (2002). https://doi.org/10.1038/nn787

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