Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/28159
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dc.contributor.authorLando, D.-
dc.contributor.authorPeet, D.-
dc.contributor.authorGorman, J.-
dc.contributor.authorWhelan, D.-
dc.contributor.authorWhitelaw, M.-
dc.contributor.authorBruick, R.-
dc.date.issued2002-
dc.identifier.citationGenes and Development, 2002; 16(12):1466-1471-
dc.identifier.issn0890-9369-
dc.identifier.issn1549-5477-
dc.identifier.urihttp://hdl.handle.net/2440/28159-
dc.description© 2002 by Cold Spring Harbor Laboratory Press-
dc.description.abstractMammalian 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.-
dc.description.statementofresponsibilityDavid Lando, Daniel J. Peet, Jeffrey J. Gorman, Dean A. Whelan, Murray L. Whitelaw and Richard K. Bruick-
dc.language.isoen-
dc.publisherCold Spring Harbor Lab Press-
dc.subjectAsparaginyl hydroxylase-
dc.subjecthypoxia-
dc.subjectoxygen sensing-
dc.subjectHIF-
dc.titleFIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor-
dc.typeJournal article-
dc.contributor.organisationCentre for the Molecular Genetics of Development-
dc.identifier.doi10.1101/gad.991402-
pubs.publication-statusPublished-
dc.identifier.orcidPeet, D. [0000-0002-6085-8936]-
Appears in Collections:Aurora harvest 2
Centre for the Molecular Genetics of Development publications
Molecular and Biomedical Science publications

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