Relating ligand binding to activation gating in CNGA2 channels

Christoph Biskup, Jana Kusch, Eckhard Schulz, Vasilica Nache, Frank Schwede, Frank Lehmann, Volker Hagen and Klaus Benndorf ()
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Christoph Biskup: Institut für Physiologie II, Friedrich-Schiller-Universität Jena, D 07740 Jena, Germany
Jana Kusch: Institut für Physiologie II, Friedrich-Schiller-Universität Jena, D 07740 Jena, Germany
Eckhard Schulz: Fachhochschule Schmalkalden, Fachbereich Elektrotechnik, Blechhammer, D 98574 Schmalkalden, Germany
Vasilica Nache: Institut für Physiologie II, Friedrich-Schiller-Universität Jena, D 07740 Jena, Germany
Frank Schwede: BIOLOG Life Science Institute, Flughafendamm 9A, D 28199 Bremen, Germany
Frank Lehmann: Dyomics GmbH, Winzerlaer Str. 2, D 07745 Jena, Germany
Volker Hagen: Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, D 13125 Berlin, Germany
Klaus Benndorf: Institut für Physiologie II, Friedrich-Schiller-Universität Jena, D 07740 Jena, Germany

Nature, 2007, vol. 446, issue 7134, 440-443

Abstract: Abstract Cyclic nucleotide-gated (CNG) ion channels mediate sensory signal transduction in photoreceptors and olfactory cells. Structurally, CNG channels are heterotetramers composed of either two or three homologue subunits1,2,3,4. Although it is well established that activation is a cooperative process of these subunits5, it remains unknown whether the cooperativity is generated by the ligand binding, the gating, or both, and how the subunits interact. In this study, the action of homotetrameric olfactory-type CNGA2 channels6 was studied in inside-out membrane patches by simultaneously determining channel activation and ligand binding, using the fluorescent cGMP analogue 8-DY547-cGMP as the ligand. At concentrations of 8-DY547-cGMP

Date: 2007
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DOI: 10.1038/nature05596

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