Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(99)00614-6
Title: Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis
Authors: Bushell, M.
McKendrick, L.
Jänicke, R.U. 
Clemens, M.J.
Morley, S.J.
Keywords: Apoptosis
Caspase
Eukaryotic initiation factor 4G
Issue Date: 28-May-1999
Citation: Bushell, M., McKendrick, L., Jänicke, R.U., Clemens, M.J., Morley, S.J. (1999-05-28). Caspase-3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis. FEBS Letters 451 (3) : 332-336. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(99)00614-6
Abstract: Induction of apoptosis BJAB cells is accompanied by the rapid cleavage of protein synthesis eukaryotic initiation factor 4G and the appearance of a fragment of approximately 76 kDa. Inhibition of apoptotic proteases (caspases) has previously been shown to prevent the cleavage of eukaryotic initiation factor 4G. In MCF-7 breast carcinoma cells, which are deficient in caspase-3, eukaryotic initiation factor 4G is not cleaved but in vivo expression of caspase-3 restores eukaryotic initiation factor 4G cleavage following induction of apoptosis. Recombinant caspase-3 can also cleave eukaryotic initiation factor 4G to yield the 76 kDa fragment both in cell extracts and when the eukaryotic initiation factor 4G is presented in a purified eukaryotic initiation factor 4F complex. These results indicate that caspase-3 activity is necessary and sufficient for eukaryotic initiation factor 4G degradation. Copyright (C) 1999 Federation of European Biochemical Societies.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/115625
ISSN: 00145793
DOI: 10.1016/S0014-5793(99)00614-6
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