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Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates
The transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues. Nitric oxide (NO) as a gaseous signal mediator shows a variety of important biological effects. In many instances, NO has been shown to exhibit its...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150788/ https://www.ncbi.nlm.nih.gov/pubmed/21837266 http://dx.doi.org/10.1080/19768354.2011.555183 |
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author | Lee, Eun Jeoung Shin, Sung Hwa Hyun, Sunghee Chun, Jaesun Kang, Sang Sun |
author_facet | Lee, Eun Jeoung Shin, Sung Hwa Hyun, Sunghee Chun, Jaesun Kang, Sang Sun |
author_sort | Lee, Eun Jeoung |
collection | PubMed |
description | The transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues. Nitric oxide (NO) as a gaseous signal mediator shows a variety of important biological effects. In many instances, NO has been shown to exhibit its activities via a protein S-nitrosylation mechanism in order to regulate its protein functions. With functional assays via site-directed mutagenesis, we demonstrate herein that NO induces the S-nitrosylation of TRPV4 Ca(2+) channel on the Cys(853) residue, and the S-nitrosylation of Cys(853) reduced its channel sensitivity to 4-α phorbol 12,13-didecanoate and the interaction between TRPV4 and calmodulin. A patch clamp experiment and Ca(2+) image analysis show that the S-nitrosylation of Cys(853) modulates the TRPV4 channel as an inhibitor. Thus, our data suggest a novel regulatory mechanism of TRPV4 via NO-mediated S-nitrosylation on its Cys(853) residue. |
format | Online Article Text |
id | pubmed-3150788 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-31507882011-08-09 Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates Lee, Eun Jeoung Shin, Sung Hwa Hyun, Sunghee Chun, Jaesun Kang, Sang Sun Animal Cells Syst (Seoul) Research Article The transient receptor potential vanilloid 4 (TRPV4) cation channel, a member of the TRP vanilloid subfamily, is expressed in a broad range of tissues. Nitric oxide (NO) as a gaseous signal mediator shows a variety of important biological effects. In many instances, NO has been shown to exhibit its activities via a protein S-nitrosylation mechanism in order to regulate its protein functions. With functional assays via site-directed mutagenesis, we demonstrate herein that NO induces the S-nitrosylation of TRPV4 Ca(2+) channel on the Cys(853) residue, and the S-nitrosylation of Cys(853) reduced its channel sensitivity to 4-α phorbol 12,13-didecanoate and the interaction between TRPV4 and calmodulin. A patch clamp experiment and Ca(2+) image analysis show that the S-nitrosylation of Cys(853) modulates the TRPV4 channel as an inhibitor. Thus, our data suggest a novel regulatory mechanism of TRPV4 via NO-mediated S-nitrosylation on its Cys(853) residue. Taylor & Francis 2011-06-09 2011-06 /pmc/articles/PMC3150788/ /pubmed/21837266 http://dx.doi.org/10.1080/19768354.2011.555183 Text en © 2011 Korean Society for Integrative Biology http://www.informaworld.com/mpp/uploads/iopenaccess_tcs.pdf This is an open access article distributed under the Supplemental Terms and Conditions for iOpenAccess articles published in Taylor & Francis journals (http://www.informaworld.com/mpp/uploads/iopenaccess_tcs.pdf) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Lee, Eun Jeoung Shin, Sung Hwa Hyun, Sunghee Chun, Jaesun Kang, Sang Sun Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title | Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title_full | Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title_fullStr | Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title_full_unstemmed | Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title_short | Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates |
title_sort | mutation of a putative s-nitrosylation site of trpv4 protein facilitates the channel activates |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3150788/ https://www.ncbi.nlm.nih.gov/pubmed/21837266 http://dx.doi.org/10.1080/19768354.2011.555183 |
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