Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel.

@article{Karttunen2015OxygendependentHB,
  title={Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel.},
  author={Sarah Karttunen and Michael David Duffield and Nathan R Scrimgeour and Lauren Squires and Wai Li Lim and Mark L Dallas and Jason L. Scragg and Johana Chicher and Keyur A. Dave and Murray L. Whitelaw and Chris Peers and Jeffrey John Gorman and Jonathan M Gleadle and G Y Rychkov and Daniel J Peet},
  journal={Journal of cell science},
  year={2015},
  volume={128 2},
  pages={
          225-31
        }
}
Factor inhibiting HIF (FIH, also known as HIF1AN) is an oxygen-dependent asparaginyl hydroxylase that regulates the hypoxia-inducible factors (HIFs). Several proteins containing ankyrin repeat domains (ARDs) have been characterised as substrates of FIH, although there is little evidence for a functional consequence of hydroxylation on these substrates. This study demonstrates that the transient receptor potential vanilloid 3 (TRPV3) channel is hydroxylated by FIH on asparagine 242 within the… CONTINUE READING

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