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Cell. 2002 Nov 27;111(5):709-20.

Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation.

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  • 1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, 151-742, Seoul, South Korea.

Abstract

Hypoxia-inducible factor 1 (HIF-1) plays a central role in cellular adaptation to changes in oxygen availability. Recently, prolyl hydroxylation was identified as a key regulatory event that targets the HIF-1alpha subunit for proteasomal degradation via the pVHL ubiquitination complex. In this report, we reveal an important function for ARD1 in mammalian cells as a protein acetyltransferase by direct binding to HIF-1alpha to regulate its stability. We present further evidence showing that ARD1-mediated acetylation enhances interaction of HIF-1alpha with pVHL and HIF-1alpha ubiquitination, suggesting that the acetylation of HIF-1alpha by ARD1 is critical to proteasomal degradation. Therefore, we have concluded that the role of ARD1 in the acetylation of HIF-1alpha provides a key regulatory mechanism underlying HIF-1alpha stability.

PMID:
12464182
[PubMed - indexed for MEDLINE]
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