Animal cells and systems

The Korean Society for Integrative Biology (한국통합생물학회)
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Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates

  • Lee, Eun-Jeoung (Department of Pre-medicine, Eulji University School of Medicine) ;
  • Shin, Sung-Hwa (Department of Biology Education, Chungbuk National University) ;
  • Hyun, Sung-Hee (Department of Pre-medicine, Eulji University School of Medicine) ;
  • Chun, Jae-Sun (Department of Biology Education, Korea National University of Education) ;
  • Kang, Sang-Sun (Department of Biology Education, Chungbuk National University)
  • Received : 2010.09.08
  • Accepted : 2010.11.01
  • Published : 2011.06.30
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Abstract

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-${\alpha}$ 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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References

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