Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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 found to copurify with PHD3 in extracts from several cell types. Our results indicate that PHD3 is a TRiC substrate, providing another step at which PHD3 activity may be regulated.

Original publication

DOI

10.1016/j.febslet.2004.06.040

Type

Journal article

Journal

FEBS Lett

Publication Date

16/07/2004

Volume

570

Pages

166 - 170

Keywords

Algorithms, Cell Line, Chaperonins, Cytosol, Dioxygenases, Edetic Acid, Electrophoresis, Polyacrylamide Gel, Gene Expression Regulation, HeLa Cells, Humans, Hypoxia, Hypoxia-Inducible Factor-Proline Dioxygenases, Immunoblotting, Oxygen, Peptides, Plasmids, Precipitin Tests, Procollagen-Proline Dioxygenase, Protein Binding, Protein Biosynthesis, Protein Structure, Tertiary, Reticulocytes, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Transfection, Trypsin