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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.

Pubmed ID: 12464182


  • Jeong JW
  • Bae MK
  • Ahn MY
  • Kim SH
  • Sohn TK
  • Bae MH
  • Yoo MA
  • Song EJ
  • Lee KJ
  • Kim KW



Publication Data

November 27, 2002

Associated Grants


Mesh Terms

  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Cell Hypoxia
  • Cell Line
  • Cell Line, Transformed
  • DNA-Binding Proteins
  • Endoribonucleases
  • Gene Expression Regulation
  • Green Fluorescent Proteins
  • Humans
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Luminescent Proteins
  • Mice
  • Molecular Sequence Data
  • Oxygen
  • Phosphoprotein Phosphatases
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Transcription Factors
  • Transcriptional Activation
  • Tumor Cells, Cultured