Presenilin 1 protein directly interacts with Bcl-2

J Biol Chem. 1999 Oct 22;274(43):30764-9. doi: 10.1074/jbc.274.43.30764.

Abstract

Presenilin proteins are involved in familial Alzheimer's disease, a neurodegenerative disorder characterized by massive death of neurons. We describe a direct interaction between presenilin 1 (PS1) and Bcl-2, a key factor in the regulation of apoptosis, by yeast two-hybrid interaction system, by co-immunoprecipitation, and by cross-linking experiments. Our data show that PS1 and Bcl-2 assemble into a macromolecular complex, and that they are released from this complex in response to an apoptotic stimulus induced by staurosporine. The results support the idea of cross-talk between these two proteins during apoptosis.

MeSH terms

  • Alzheimer Disease / physiopathology
  • Cell Line
  • Cloning, Molecular
  • HeLa Cells
  • Humans
  • In Situ Nick-End Labeling
  • Lymphocytes
  • Membrane Proteins / chemistry*
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism*
  • Presenilin-1
  • Protein Binding
  • Proto-Oncogene Proteins c-bcl-2 / chemistry*
  • Proto-Oncogene Proteins c-bcl-2 / isolation & purification
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Staurosporine / pharmacology
  • Tumor Cells, Cultured

Substances

  • Membrane Proteins
  • PSEN1 protein, human
  • Presenilin-1
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Proteins
  • Staurosporine