OS-9: another piece in the HIF complex story

Mol Cell. 2005 Feb 18;17(4):472-3. doi: 10.1016/j.molcel.2005.02.001.

Abstract

In this issue of Molecular Cell, the Semenza group reports that OS-9, a common protein of unassigned function, promotes the O2-dependent degradation of hypoxia inducible factor (HIF) via binding to both HIF and the HIF prolyl-hydroxylases, implying that OS-9 is part of a multiprotein complex involved in the hypoxic response (Baek et al., 2005).

Publication types

  • Review

MeSH terms

  • Cell Hypoxia*
  • Humans
  • Hydroxylation
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Lectins
  • Neoplasm Proteins / metabolism*
  • Oxygen / metabolism*
  • Procollagen-Proline Dioxygenase / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Tumor Suppressor Proteins / metabolism*
  • Ubiquitin-Protein Ligases / metabolism*
  • Von Hippel-Lindau Tumor Suppressor Protein

Substances

  • HIF1A protein, human
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Lectins
  • Neoplasm Proteins
  • OS9 protein, human
  • Transcription Factors
  • Tumor Suppressor Proteins
  • Procollagen-Proline Dioxygenase
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein
  • Proteasome Endopeptidase Complex
  • VHL protein, human
  • Oxygen