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Type: Journal article
Title: Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel
Author: Karttunen, S.
Duffield, M.
Scrimgeour, N.
Squires, L.
Lim, W.
Dallas, M.
Scragg, J.
Chicher, J.
Dave, K.
Whitelaw, M.
Peers, C.
Gorman, J.
Gleadle, J.
Rychkov, G.
Peet, D.
Citation: Journal of Cell Science, 2015; 128(2):225-231
Publisher: Company of Biologists
Issue Date: 2015
ISSN: 0021-9533
Statement of
Sarah Karttunen, Michael Duffield, Nathan R. Scrimgeour, Lauren Squires, Wai Li Lim, Mark L. Dallas, Jason L. Scragg, Johana Chicher, Keyur A. Dave, Murray L. Whitelaw, Chris Peers, Jeffrey J. Gorman, Jonathan M. Gleadle, Grigori Y. Rychkov, and Daniel J. Peet
Abstract: 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 cytoplasmic ARD. Hypoxia, FIH inhibitors and mutation of asparagine 242 all potentiated TRPV3-mediated current, without altering TRPV3 protein levels, indicating that oxygen-dependent hydroxylation inhibits TRPV3 activity. This novel mechanism of channel regulation by oxygen-dependent asparaginyl hydroxylation is likely to extend to other ion channels.
Keywords: FIH
Rights: © 2015.
DOI: 10.1242/jcs.158451
Appears in Collections:Aurora harvest 7
Molecular and Biomedical Science publications

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