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KMID : 1161520110150020095
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Animal Cells and Systems
2011 Volume.15 No. 2 p.95 ~ p.106
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Mutation of a putative S-nitrosylation site of TRPV4 protein facilitates the channel activates
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Lee Eun-Jeoung
Shin Sung-Hwa
Hyun Sung-Hee
Chun Jae-Sun
Kang Sang-Sun
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Abstract
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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 Ca2+channel on the Cys853 residue, and the S-nitrosylation of Cys853 reduced its channel sensitivity to 4-α phorbol 12,13-didecanoate and the interaction between TRPV4 and calmodulin. A patch clamp experiment and Ca2+ image analysis show that the S-nitrosylation of Cys853 modulates the TRPV4 channel as an inhibitor. Thus, our data suggest a novel regulatory mechanism of TRPV4 via NO-mediated S-nitrosylation on its Cys853 residue.
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KEYWORD
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TRPV4, NO, S-nitrosylation, 4-aphorbol 12, 13-didecanoate, Ca2channel, protein-protein interaction
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