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

被引：49

作者：

Masson, N

Appelhoff, RJ

Tuckerman, JR

Tian, Y

Demol, H

Puype, M

Vandekerckhove, J

Ratcliffe, PJ

Pugh, CW

机构：

[1] Henry Wellcome Bldg Genom Med, Oxford OX3 7BN, England

[2] State Univ Ghent VIB, Fac Med & Hlth Sci, Dept Med Prot Res, B-9000 Ghent, Belgium

来源：

FEBS LETTERS | 2004年 / 570卷 / 1-3期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

prolyl hydroxylase; protein folding; TRiC chaperonin;

D O I：

10.1016/j.febslet.2004.06.040

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

收藏

页码：166 / 170

页数：5

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