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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Jeong, J.W., Bae, M.K., Ahn, M.Y., Kim, S.H., Sohn, T.K., Bae, M.H., Yoo, M.A., Song, E.J., Lee, K.J., Kim, K.W. Cell (2002) [Pubmed]
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