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https://hdl.handle.net/2440/28159
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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 1549-5477 |
Organisation: | Centre for the Molecular Genetics of Development |
Statement of Responsibility: | 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 hypoxia oxygen sensing HIF |
Description: | © 2002 by Cold Spring Harbor Laboratory Press |
DOI: | 10.1101/gad.991402 |
Published version: | http://dx.doi.org/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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