- Abstract:
-
The stability and activity of hypoxia-inducible factor (HIF) are regulated by the post-translational hydroxylation of specific prolyl and asparaginyl residues. We show that the HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also catalyzes hydroxylation of highly conserved asparaginyl residues within ankyrin repeat (AR) domains (ARDs) of endogenous Notch receptors. AR hydroxylation decreases the extent of ARD binding to FIH while not affecting signaling through the canonical Notch p...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.m704102200
-
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- Journal:
- The Journal of biological chemistry
- Volume:
- 282
- Issue:
- 33
- Pages:
- 24027-24038
- Publication date:
- 2007-08-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- URN:
-
uuid:74826a6b-6a38-4c6a-a6bd-6253c0621f10
- Source identifiers:
-
18302
- Local pid:
- pubs:18302
- Copyright date:
- 2007
Journal article
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
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