1. Author Correction: The ASIC3/P2X3 cognate receptor is a pain-relevant and ligand-gated cationic channel
- Author
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Wolfgang Nörenberg, Ye Yu, Sandra Vilotti, Anke Dopychai, Beáta Sperlágh, Heike Franke, Gabriele Stephan, Yong Tang, Elsa Fabbretti, Patrizia Rubini, Ralf Hausmann, Günther Schmalzing, Flóra Gölöncsér, Peter Illes, and Lumei Huang
- Subjects
0301 basic medicine ,Flora ,Multidisciplinary ,Science ,Published Erratum ,Philosophy ,General Physics and Astronomy ,General Chemistry ,Article ,General Biochemistry, Genetics and Molecular Biology ,Linguistics ,03 medical and health sciences ,030104 developmental biology ,ComputingMethodologies_DOCUMENTANDTEXTPROCESSING ,Ligand-gated ion channel ,lcsh:Q ,Cognate ,lcsh:Science - Abstract
Two subclasses of acid-sensing ion channels (ASIC3) and of ATP-sensitive P2X receptors (P2X3Rs) show a partially overlapping expression in sensory neurons. Here we report that both recombinant and native receptors interact with each other in multiple ways. Current measurements with the patch-clamp technique prove that ASIC3 stimulation strongly inhibits the P2X3R current partly by a Ca2+-dependent mechanism. The proton-binding site is critical for this effect and the two receptor channels appear to switch their ionic permeabilities during activation. Co-immunoprecipation proves the close association of the two protein structures. BN-PAGE and SDS-PAGE analysis is also best reconciled with the view that ASIC3 and P2X3Rs form a multiprotein structure. Finally, in vivo measurements in rats reveal the summation of pH and purinergically induced pain. In conclusion, the receptor subunits do not appear to form a heteromeric channel, but tightly associate with each other to form a protein complex, mediating unidirectional inhibition., Two subclasses of ligand-gated ion channels (ASIC3 and P2X3) are both present at sensory neurons and might be therefore subject to receptor crosstalk. Here authors use electrophysiology, biochemistry and co-immunoprecipitation to show that the two ion channels interact and affect P2X3 currents.
- Published
- 2018