Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel|
|Citation:||Journal of Cell Science, 2015; 128(2):225-231|
|Publisher:||Company of Biologists|
|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.|
|Appears in Collections:||Aurora harvest 7|
Molecular and Biomedical Science publications
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.