Regulation of Pim-1 by Hsp90

Biochem Biophys Res Commun. 2001 Mar 2;281(3):663-9. doi: 10.1006/bbrc.2001.4405.

Abstract

The protooncogene Pim-1 encodes serine/threonine protein kinases that are involved in cytokine-mediated cell proliferation and in lymphoma- and leukemogenesis. It is largely unknown how Pim-1 executes its biological effects. Here we show that Pim-1 physically interacts with heat shock protein 90 alpha and beta (Hsp90alpha and beta). The Hsp90-specific inhibitor geldanamycin (GA) induced a rapid degradation of Pim-1 and reduced its kinase activity. The expression of Hsp90alpha was regulated by a signal from the cytokine receptor gp130, as is Pim-1's expression. These results indicate that Hsp90 is coordinately regulated with Pim-1 and is involved in the stabilization and function of Pim-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, CD / metabolism
  • Base Sequence
  • Cell Line
  • Cytokine Receptor gp130
  • DNA Primers
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation / physiology*
  • HSP90 Heat-Shock Proteins / physiology*
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins c-pim-1
  • Reverse Transcriptase Polymerase Chain Reaction
  • STAT3 Transcription Factor
  • Signal Transduction
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Trans-Activators / metabolism

Substances

  • Antigens, CD
  • DNA Primers
  • DNA-Binding Proteins
  • HSP90 Heat-Shock Proteins
  • Membrane Glycoproteins
  • Proto-Oncogene Proteins
  • STAT3 Transcription Factor
  • Trans-Activators
  • Cytokine Receptor gp130
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-pim-1