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

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 in...

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Bibliographic Details
Published in:FEBS letters 2004-07, Vol.570 (1), p.166-170
Main Authors: Masson, Norma, Appelhoff, Rebecca J., Tuckerman, Jason R., Tian, Ya-min, Demol, Hans, Puype, Magda, Vandekerckhove, Joel, Ratcliffe, Peter J., Pugh, Christopher W.
Format: Article
Language:English
Subjects:
Algorithms
Cell Line
Chaperonins - chemistry
Cytosol - metabolism
Dioxygenases
Edetic Acid - pharmacology
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation
HeLa Cells
Humans
Hypoxia
Hypoxia-Inducible Factor-Proline Dioxygenases
Immunoblotting
Oxygen - metabolism
Peptides - chemistry
Plasmids - metabolism
Precipitin Tests
Procollagen-Proline Dioxygenase - chemistry
Procollagen-Proline Dioxygenase - physiology
Prolyl hydroxylase
Protein Binding
Protein Biosynthesis
Protein folding
Protein Structure, Tertiary
Reticulocytes - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Transfection
TRiC chaperonin
Trypsin - chemistry
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2004.06.040