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Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis.

Growth factor suppression of apoptosis correlates with the phosphorylation and inactivation of multiple proapoptotic proteins, including the BCL-2 family member BAD. However, the physiological events required for growth factors to block cell death are not well characterized. To assess the contribution of BAD inactivation to cell survival, we generated mice with point mutations in the BAD gene that abolish BAD phosphorylation at specific sites. We show that BAD phosphorylation protects cells from the deleterious effects of apoptotic stimuli and attenuates death pathway signaling by raising the threshold at which mitochondria release cytochrome c to induce cell death. These findings establish a function for endogenous BAD phosphorylation, and elucidate a mechanism by which survival kinases block apoptosis in vivo.

Pubmed ID: 12431371


  • Datta SR
  • Ranger AM
  • Lin MZ
  • Sturgill JF
  • Ma YC
  • Cowan CW
  • Dikkes P
  • Korsmeyer SJ
  • Greenberg ME


Developmental cell

Publication Data

November 14, 2002

Associated Grants

  • Agency: NICHD NIH HHS, Id: P01 HD24926
  • Agency: NICHD NIH HHS, Id: P30-HD18655
  • Agency: NCI NIH HHS, Id: R37CA50239

Mesh Terms

  • Animals
  • Apoptosis
  • B-Lymphocytes
  • Carrier Proteins
  • Cell Differentiation
  • Cell Survival
  • Cells, Cultured
  • Cytochrome c Group
  • DNA-Binding Proteins
  • Fibroblasts
  • Hematopoietic Stem Cells
  • Insulin-Like Growth Factor I
  • Mice
  • Mice, Inbred C57BL
  • Mitochondria
  • Neurons
  • Phosphorylation
  • Platelet-Derived Growth Factor
  • Proto-Oncogene Proteins c-bcl-2
  • Signal Transduction
  • T-Lymphocytes
  • Thymus Gland
  • Transcription Factors
  • bcl-Associated Death Protein