CREB is cleaved by caspases during neural cell apoptosis

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Abstract

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
Volume486
Issue number3
DOIs
StatePublished - Dec 15 2000

Funding

We thank Gretchen McCaffrey and Max Scott for comments and input, and Michael Comb for antibodies to CREB. F.F. was supported by an A.M. and G.L. Wilson grant from the Palmerston North Medical Research Foundation, a Health Research Council of New Zealand Postgraduate Scholarship, and New Zealand Vice-Chancellors’ Committee Georgetti and Shirtcliffe Fellowships. This work was supported by the Whitehall Foundation (USA) and the following New Zealand sources: The Cancer Society, Health Research Council, Lottery Health and Lottery Science, Neurological Foundation, National Child Health Research Foundation, and the Real Kids Charitable Trust.

Funders
Nepal Health Research Council

    Keywords

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

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