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Caspase cleavage of the transcription factor FLI-1 during preB leukemic cell death

Sandrine Sarrazin1, Christelle Bonod-Bidaud, Pierre Remy

  • 1Transcription/Différenciation Hématopoïétique and Apoptose/Différenciation, label la ligue contre le cancer-Centre de Génétique Moléculaire et Cellulaire, CNRS UMR 5534, 43 Boulevard du 11 Novembre 1918, 69622 Villeurbanne, France.

Biochimica Et Biophysica Acta
|October 16, 2002
PubMed

Insights

The transcription factor FLI-1, which normally prevents programmed cell death (apoptosis), is cleaved by caspases during apoptosis. This caspase cleavage of FLI-1 may be crucial for initiating irreversible cell death.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Programmed cell death (apoptosis) is a vital cellular process regulated by caspases and apoptosis-regulating proteins.
  • The ETS-family transcription factor FLI-1 exhibits anti-apoptotic activity and is implicated in malignant transformation.

Purpose of the Study:

  • To investigate the role of FLI-1 cleavage by caspases during apoptosis in murine preB leukemic cells.
  • To determine if caspase cleavage of FLI-1 is a conserved mechanism for regulating cell death.

Main Methods:

  • Analysis of FLI-1 cleavage during apoptosis in murine preB leukemic cells.
  • In vitro cleavage assays using purified caspase 3 and FLI-1 isoforms.

Main Results:

  • Apoptosis in murine preB leukemic cells involves specific cleavage of FLI-1 by caspase-like activity.
  • Two FLI-1 isoforms are cleaved at three conserved sites by caspase 3 in vitro.
  • Conserved cleavage sites suggest a critical role in ensuring irreversible cell death.

Conclusions:

  • Caspase-mediated cleavage of the anti-apoptotic factor FLI-1 is a key event in programmed cell death.
  • This cleavage mechanism is conserved across species, highlighting its importance in regulating cell fate.

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