Calcineurin promotes hypoxia-inducible factor 1alpha expression by dephosphorylating RACK1 and blocking RACK1 dimerization

J Biol Chem. 2007 Dec 21;282(51):37064-73. doi: 10.1074/jbc.M705015200. Epub 2007 Oct 26.

Abstract

Oxygen homeostasis represents an essential organizing principle of metazoan evolution and biology. Hypoxia-inducible factor 1 (HIF-1) is a master regulator of transcriptional responses to changes in O2 concentration. HIF-1 is a heterodimer of HIF-1alpha and HIF-1beta subunits. O2-dependent degradation of the HIF-1alpha subunit is mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin ligase, and the proteasome. O2-independent degradation of HIF-1alpha is regulated by the competition of RACK1 and HSP90 for binding to HIF-1alpha. RACK1 binding results in the recruitment of the Elongin-C E3 ubiquitin ligase, leading to VHL-independent ubiquitination and degradation of HIF-1alpha. In this report, we show that calcineurin inhibits the ubiquitination and proteasomal degradation of HIF-1alpha. Calcineurin is a serine/threonine phosphatase that is activated by calcium and calmodulin. The phosphatase activity of calcineurin is required for its regulation of HIF-1alpha. RACK1 binds to the catalytic domain of calcineurin and is required for HIF-1alpha degradation induced by the calcineurin inhibitor cyclosporine A. Elongin-C and HIF-1alpha each bind to RACK1 and dimerization of RACK1 is required to recruit Elongin-C to HIF-1alpha. Phosphorylation of RACK1 promotes its dimerization and dephosphorylation by calcineurin inhibits dimerization. Serine 146 within the dimerization domain is phosphorylated and mutation of serine 146 impairs RACK1 dimerization and HIF-1alpha degradation. These results indicate that intracellular calcium levels can regulate HIF-1alpha expression by modulating calcineurin activity and RACK1 dimerization.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aryl Hydrocarbon Receptor Nuclear Translocator / metabolism
  • Calcineurin / metabolism*
  • Calcium / metabolism*
  • Calmodulin / metabolism*
  • Cell Line
  • Cyclosporine / pharmacology
  • Dimerization
  • Elongin
  • Enzyme Activation / drug effects
  • Enzyme Activation / physiology
  • Enzyme Inhibitors / pharmacology
  • GTP-Binding Proteins / metabolism*
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology*
  • HSP90 Heat-Shock Proteins / metabolism
  • Humans
  • Hypoxia-Inducible Factor 1, alpha Subunit / biosynthesis*
  • Neoplasm Proteins / metabolism*
  • Oxygen / metabolism
  • Oxygen Consumption / drug effects
  • Oxygen Consumption / physiology
  • Phosphorylation / drug effects
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • Protein Structure, Tertiary / physiology
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface / metabolism*
  • Transcription Factors / metabolism
  • Ubiquitin / metabolism
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination / drug effects
  • Ubiquitination / physiology
  • Von Hippel-Lindau Tumor Suppressor Protein / metabolism

Substances

  • ARNT protein, human
  • Calmodulin
  • ELOC protein, human
  • Elongin
  • Enzyme Inhibitors
  • HIF1A protein, human
  • HSP90 Heat-Shock Proteins
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Neoplasm Proteins
  • RACK1 protein, human
  • Receptors for Activated C Kinase
  • Receptors, Cell Surface
  • Transcription Factors
  • Ubiquitin
  • Aryl Hydrocarbon Receptor Nuclear Translocator
  • Cyclosporine
  • Ubiquitin-Protein Ligases
  • Von Hippel-Lindau Tumor Suppressor Protein
  • Calcineurin
  • Proteasome Endopeptidase Complex
  • GTP-Binding Proteins
  • VHL protein, human
  • Oxygen
  • Calcium