Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α
Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α
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DOI：
10.1016/j.febslet.2005.10.036
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发表时间：
2005-11-21
期刊：
影响因子：
3.5
通讯作者：
Lillehaug, JR
中科院分区：
文献类型：
--
作者：
Arnesen, T;Kong, X;Lillehaug, JR
缺氧诱导因子-1 α（HIF-1 α）是细胞对缺氧反应的核心成分。低氧条件导致HIF-1 α的稳定（和转录活性HIF-1复合物的形成）。有人认为，哺乳动物ARD 1乙酰化HIF-1 α，从而增强HIF-1 α泛素化和降解。此外，ARD 1被认为在缺氧中下调，从而促进HIF-1 α的稳定。在这里，我们证明了人类ARD 1（hARD 1）蛋白的水平在缺氧中不会降低。此外，hARD 1不乙酰化和不稳定HIF-1 α。然而，我们发现hARD 1特异性结合HIF-1 α，这表明这些蛋白质之间存在推定的，但仍不清楚的联系。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Hypoxia inducible factor-1 alpha (HIF-1 alpha) is a central component of the cellular responses to hypoxia. Hypoxic conditions result in stabilization of HIF-1 alpha( and formation of the transcriptionally active HIF-1 complex. It was suggested that mammalian ARD1 acetylates HIF-1 alpha and thereby enhances HIF-1 alpha ubiquitination and degradation. Furthermore, ARD1 was proposed to be downregulated in hypoxia thus facilitating the stabilization of HIF-1 alpha. Here we demonstrate that the level of human ARD1 (hARD1) protein is not decreased in hypoxia. Moreover, hARD1 does not acetylate and destabilize HIF-1 alpha. However, we find that hARD1 specifically binds HIF-1 alpha, suggesting a putative, still unclear, connection between these proteins. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.