The HIF prolyl hydroxylase PHD3 is a potential substrate of the TRiC chaperonin.

Journal article

Hypoxia-inducible factor-1 (HIF) is regulated by oxygen-dependent prolyl hydroxylation. Of the three HIF prolyl hydroxylases (PHD1, 2 and 3) identified, PHD3 exhibits restricted substrate specificity in vitro and is induced in different cell types by diverse stimuli. PHD3 may therefore provide an interface between oxygen sensing and other signalling pathways. We have used co-purification and mass spectrometry to identify proteins that interact with PHD3. The cytosolic chaperonin TRiC was foun...

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Authors: Masson, N; Appelhoff, R; Tuckerman, JR; Tian, Y; Demol, H

• Publication status: Published
• Journal: FEBS letters
• Volume: 570
• Issue: 1-3
• Pages: 166-170
• Publication date: 2004-07-01
• DOI: 10.1016/j.febslet.2004.06.040
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Reticulocytes; Protein Structure, Tertiary; Peptides; Cytosol; Gene Expression Regulation; Chaperonins; Procollagen-Proline Dioxygenase; Edetic Acid; Cell Line; Algorithms; Oxygen; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Protein Biosynthesis; Trypsin; Precipitin Tests; Anoxia; Humans; Protein Binding; Dioxygenases; Electrophoresis, Polyacrylamide Gel; Immunoblotting; Transfection; Plasmids; Hela Cells