Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor|
|Citation:||Genes and Development, 2002; 16(12):1466-1471|
|Publisher:||Cold Spring Harbor Lab Press|
|Organisation:||Centre for the Molecular Genetics of Development|
|David Lando, Daniel J. Peet, Jeffrey J. Gorman, Dean A. Whelan, Murray L. Whitelaw and Richard K. Bruick|
|Abstract:||Mammalian cells adapt to hypoxic conditions through a transcriptional response pathway mediated by the hypoxia-inducible factor, HIF. HIF transcriptional activity is suppressed under normoxic conditions by hydroxylation of an asparagine residue within its C-terminal transactivation domain, blocking association with coactivators. Here we show that the protein FIH-1, previously shown to interact with HIF, is an asparaginyl hydroxylase. Like known hydroxylase enzymes, FIH-1 is an Fe(II)-dependent enzyme that uses molecular O(2) to modify its substrate. Together with the recently discovered prolyl hydroxylases that regulate HIF stability, this class of oxygen-dependent enzymes comprises critical regulatory components of the hypoxic response pathway.|
|Description:||© 2002 by Cold Spring Harbor Laboratory Press|
|Appears in Collections:||Aurora harvest 2|
Centre for the Molecular Genetics of Development publications
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.