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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...

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Autores principales: Lee, Eun Jeoung, Shin, Sung Hwa, Hyun, Sunghee, Chun, Jaesun, Kang, Sang Sun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2011
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.
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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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