FIH-Dependent Asparaginyl Hydroxylation of Ankyrin Repeat Domain-Containing Proteins

被引：70

作者：

Cockman, Matthew E. ^{[1
]}

Webb, James D. ^{[1
]}

Ratcliffe, Peter J. ^{[1
]}

机构：

[1] Univ Oxford, Oxford, England

来源：

HYPOXIA AND CONSEQUENCES FROM MOLECULE TO MALADY | 2009年 / 1177卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

factor inhibiting HIF (FIH); hypoxia; ankyrin repeat domain (ARD); posttranslational hydroxylation; STRUCTURAL BASIS; SUBSTRATE; NOTCH; ACCUMULATION;

D O I：

10.1111/j.1749-6632.2009.05042.x

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Studies on hypoxia-sensitive pathways have identified a series of Fe(II)-dependent dioxygenases that regulate hypoxia-inducible factor (HIF) by prolyl and asparaginyl hydroxylation. The asparaginyl hydroxylase factor inhibiting HIF (FIH) targets a conserved asparaginyl residue in the C-terminal transactivation domain of HIF-alpha. This modification suppresses HIF transcriptional activity by inhibiting co-activator recruitment. Recent work has demonstrated that FIH targets an alternative class of substrate. Proteins containing a common interaction motif known as the ankyrin repeat domain (ARD) have been shown to be efficiently hydroxylated by FIH. This review aims to summarize what is currently known regarding ARD hydroxylation, including the kinetics and determinants of FIH-mediated ARD hydroxylation, the structural and functional consequences of ARD hydroxylation, and the potential for cross-talk between ARD proteins and HIF signaling.

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页码：9 / 18

页数：10

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