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Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.

Abstract:

HIF (hypoxia-inducible factor) is an alphabeta transcription factor that modulates the hypoxic response in many animals. The cellular abundance and activity of HIF-alpha are regulated by its post-translational hydroxylation. The hydroxylation of HIF is catalysed by PHD (prolyl hydroxylase domain) enzymes and FIH (factorinhibiting HIF), all of which are 2-oxoglutarate- and Fe(II)-dependent dioxygenases. FIH hydroxylates a conserved asparagine residue in HIF-alpha (Asn-803), which blocks the bi...

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Publication status:
Published

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Publisher copy:
10.1042/BJ20040735

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Journal:
The Biochemical journal
Volume:
383
Issue:
Pt. 3
Pages:
429-437
Publication date:
2004-11-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:f8c66263-9aa3-49bd-a41b-37568ae8bf88
Source identifiers:
21948
Local pid:
pubs:21948

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