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Caspase‐3 is necessary and sufficient for cleavage of protein synthesis eukaryotic initiation factor 4G during apoptosis
Author(s) -
Bushell Martin,
McKendrick Linda,
Jänicke Reiner U.,
Clemens Michael J.,
Morley Simon J.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00614-6
Subject(s) - eukaryotic initiation factor , caspase , cleavage (geology) , eif4a1 , microbiology and biotechnology , initiation factor , eukaryotic translation initiation factor 4 gamma , apoptosis , biology , proteases , cleavage stimulation factor , cleavage factor , programmed cell death , biochemistry , enzyme , gene , messenger rna , translation (biology) , paleontology , fracture (geology)
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.