CREB is cleaved by caspases during neural cell apoptosis

Fleur François, Maria J. Godinho, Mark L. Grimes

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Programmed cell death, or apoptosis, is a tightly regulated process mediated by selective cleavage of proteins by caspases, resulting in ordered destruction of the cell. In addition to structural proteins, proteins that mediate anti-apoptotic signal transduction are also substrates; their destruction eliminates potential futile attempts to escape execution. We asked whether cAMP response element binding protein (CREB), a transcription factor that mediates nerve growth factor (NGF) survival signals, is a target for caspases during apoptosis. CREB was specifically cleaved by caspases in neuroblastoma extracts, and in cells induced to undergo apoptosis by staurosporine. The destruction of CREB eliminates a key factor that could reverse apoptosis. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)281-284
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - Dec 15 2000


  • Apoptosis
  • Caspase
  • In vitro reconstitution
  • Neuroblastoma
  • Signal transduction
  • cAMP response element binding protein


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