4.5 Article

Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α

Journal

FEBS LETTERS
Volume 579, Issue 28, Pages 6428-6432

Publisher

WILEY
DOI: 10.1016/j.febslet.2005.10.036

Keywords

protein acetylation; acetyltransferase; hypoxia inducible factor-1 alpha; hypoxia; human ARD1; degradation

Funding

  1. NCI NIH HHS [K01 CA098809] Funding Source: Medline

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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.

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