Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function

Oncogene. 2003 Oct 2;22(43):6785-93. doi: 10.1038/sj.onc.1206792.

Abstract

Bim is a proapoptotic member of the Bcl-2 family that shares only the BH3 domain with this family. Three Bim proteins Bim-EL, Bim-L and Bim-S are synthesized from the same transcript. We report here that Bim-EL when phosphorylated by Erk1/2 is rapidly degraded via the proteasome pathway. Using different cellular models we evidence that serine 69 is both necessary and sufficient for Erk1/2-mediated phosphorylation and degradation of Bim-EL. In K562 cells, Phorbol 12-myristate 13-acetate activates Erk1/2 and consequently increases Bim-EL phosphorylation and degradation by the proteasome, resulting in cell survival, while the Bcr-Abl inhibitor imatinib abrogates Bim-EL phosphorylation and degradation and induces caspase activation and apoptosis. We also show that Bim-EL(S69G) promotes apoptosis more efficiently than Bim-EL-WT in K562 cells. Altogether, our findings demonstrate that phosphorylation of Bim-EL by Erk1/2 on serine 69 selectively leads to its proteasomal degradation and therefore represents a new and important mechanism of Bim regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antineoplastic Agents, Hormonal / pharmacology
  • Apoptosis Regulatory Proteins
  • Apoptosis*
  • Bcl-2-Like Protein 11
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Caspases / metabolism
  • Cell Line
  • Cell Survival
  • Cysteine Endopeptidases / metabolism*
  • Gene Expression Regulation
  • Glutathione Transferase / metabolism
  • Humans
  • K562 Cells
  • Lymphoma / metabolism
  • Membrane Proteins*
  • Mitogen-Activated Protein Kinase 1 / metabolism*
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases / metabolism*
  • Models, Biological
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Phosphorylation
  • Proteasome Endopeptidase Complex
  • Protein Isoforms
  • Proto-Oncogene Proteins c-raf / metabolism
  • Proto-Oncogene Proteins*
  • Serine / chemistry*
  • Tamoxifen / pharmacology
  • Tetradecanoylphorbol Acetate
  • Time Factors
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents, Hormonal
  • Apoptosis Regulatory Proteins
  • BCL2L11 protein, human
  • Bcl-2-Like Protein 11
  • Carrier Proteins
  • Membrane Proteins
  • Multienzyme Complexes
  • Protein Isoforms
  • Proto-Oncogene Proteins
  • Tamoxifen
  • Serine
  • Glutathione Transferase
  • Proto-Oncogene Proteins c-raf
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • Caspases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Tetradecanoylphorbol Acetate