The ASIC3/P2X3 cognate receptor is a pain-relevant and ligand-gated cationic channel View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Gabriele Stephan, Lumei Huang, Yong Tang, Sandra Vilotti, Elsa Fabbretti, Ye Yu, Wolfgang Nörenberg, Heike Franke, Flóra Gölöncsér, Beáta Sperlágh, Anke Dopychai, Ralf Hausmann, Günther Schmalzing, Patrizia Rubini, Peter Illes

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. More... »

PAGES

1354

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-018-03728-5

DOI

http://dx.doi.org/10.1038/s41467-018-03728-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1103202197

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29636447


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