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Type: Journal article
Title: FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
Author: Lando, D.
Peet, D.
Gorman, J.
Whelan, D.
Whitelaw, M.
Bruick, R.
Citation: Genes and Development, 2002; 16(12):1466-1471
Publisher: Cold Spring Harbor Lab Press
Issue Date: 2002
ISSN: 0890-9369
Organisation: Centre for the Molecular Genetics of Development
Statement of
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.
Keywords: Asparaginyl hydroxylase
oxygen sensing
Description: © 2002 by Cold Spring Harbor Laboratory Press
DOI: 10.1101/gad.991402
Appears in Collections:Aurora harvest 2
Centre for the Molecular Genetics of Development publications
Molecular and Biomedical Science publications

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