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Deciphering the function of the CNGB1b subunit in olfactory CNG channels
Olfactory cyclic nucleotide-gated (CNG) ion channels are key players in the signal transduction cascade of olfactory sensory neurons. The second messengers cAMP and cGMP directly activate these channels, generating a depolarizing receptor potential. Olfactory CNG channels are composed of two CNGA2 s...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4942689/ https://www.ncbi.nlm.nih.gov/pubmed/27405959 http://dx.doi.org/10.1038/srep29378 |
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author | Nache, Vasilica Wongsamitkul, Nisa Kusch, Jana Zimmer, Thomas Schwede, Frank Benndorf, Klaus |
author_facet | Nache, Vasilica Wongsamitkul, Nisa Kusch, Jana Zimmer, Thomas Schwede, Frank Benndorf, Klaus |
author_sort | Nache, Vasilica |
collection | PubMed |
description | Olfactory cyclic nucleotide-gated (CNG) ion channels are key players in the signal transduction cascade of olfactory sensory neurons. The second messengers cAMP and cGMP directly activate these channels, generating a depolarizing receptor potential. Olfactory CNG channels are composed of two CNGA2 subunits and two modulatory subunits, CNGA4, and CNGB1b. So far the exact role of the modulatory subunits for channel activation is not fully understood. By measuring ligand binding and channel activation simultaneously, we show that in functional heterotetrameric channels not only the CNGA2 subunits and the CNGA4 subunit but also the CNGB1b subunit binds cyclic nucleotides and, moreover, also alone translates this signal to open the pore. In addition, we show that the CNGB1b subunit is the most sensitive subunit in a heterotetrameric channel to cyclic nucleotides and that it accelerates deactivation to a similar extent as does the CNGA4 subunit. In conclusion, the CNGB1b subunit participates in ligand-gated activation of olfactory CNG channels and, particularly, contributes to rapid termination of odorant signal in an olfactory sensory neuron. |
format | Online Article Text |
id | pubmed-4942689 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-49426892016-07-20 Deciphering the function of the CNGB1b subunit in olfactory CNG channels Nache, Vasilica Wongsamitkul, Nisa Kusch, Jana Zimmer, Thomas Schwede, Frank Benndorf, Klaus Sci Rep Article Olfactory cyclic nucleotide-gated (CNG) ion channels are key players in the signal transduction cascade of olfactory sensory neurons. The second messengers cAMP and cGMP directly activate these channels, generating a depolarizing receptor potential. Olfactory CNG channels are composed of two CNGA2 subunits and two modulatory subunits, CNGA4, and CNGB1b. So far the exact role of the modulatory subunits for channel activation is not fully understood. By measuring ligand binding and channel activation simultaneously, we show that in functional heterotetrameric channels not only the CNGA2 subunits and the CNGA4 subunit but also the CNGB1b subunit binds cyclic nucleotides and, moreover, also alone translates this signal to open the pore. In addition, we show that the CNGB1b subunit is the most sensitive subunit in a heterotetrameric channel to cyclic nucleotides and that it accelerates deactivation to a similar extent as does the CNGA4 subunit. In conclusion, the CNGB1b subunit participates in ligand-gated activation of olfactory CNG channels and, particularly, contributes to rapid termination of odorant signal in an olfactory sensory neuron. Nature Publishing Group 2016-07-11 /pmc/articles/PMC4942689/ /pubmed/27405959 http://dx.doi.org/10.1038/srep29378 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Nache, Vasilica Wongsamitkul, Nisa Kusch, Jana Zimmer, Thomas Schwede, Frank Benndorf, Klaus Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title | Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title_full | Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title_fullStr | Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title_full_unstemmed | Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title_short | Deciphering the function of the CNGB1b subunit in olfactory CNG channels |
title_sort | deciphering the function of the cngb1b subunit in olfactory cng channels |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4942689/ https://www.ncbi.nlm.nih.gov/pubmed/27405959 http://dx.doi.org/10.1038/srep29378 |
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