Translation initiation factor modifications and the regulation of protein synthesis in apoptotic cells
The rate of protein synthesis is rapidly down-regulated in mammalian cells following the induction of apoptosis. Inhibition occurs at the level of polypeptide chain initiation and is accompanied by the phosphorylation of the alpha subunit of initiation factor eIF2 and the caspase-dependent cleavage...
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| Veröffentlicht in: | Cell death and differentiation 2000-07, Vol.7 (7), p.603-615 |
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| container_title | Cell death and differentiation |
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| creator | Clemens, M J Bushell, M Jeffrey, I W Pain, V M Morley, S J |
| description | The rate of protein synthesis is rapidly down-regulated in mammalian cells following the induction of apoptosis. Inhibition occurs at the level of polypeptide chain initiation and is accompanied by the phosphorylation of the alpha subunit of initiation factor eIF2 and the caspase-dependent cleavage of initiation factors eIF4G, eIF4B, eIF2alpha and the p35 subunit of eIF3. Proteolytic cleavage of these proteins yields characteristic products which may exert regulatory effects on the translational machinery. Inhibition of caspase activity protects protein synthesis from long-term inhibition in cells treated with some, but not all, inducers of apoptosis. This review describes the initiation factor modifications and the possible signalling pathways by which translation may be regulated during apoptosis. We discuss the significance of the initiation factor cleavages and other changes for protein synthesis, and the implications of these events for our understanding of the cellular changes associated with apoptosis. |
| doi_str_mv | 10.1038/sj.cdd.4400695 |
| format | Article |
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Inhibition occurs at the level of polypeptide chain initiation and is accompanied by the phosphorylation of the alpha subunit of initiation factor eIF2 and the caspase-dependent cleavage of initiation factors eIF4G, eIF4B, eIF2alpha and the p35 subunit of eIF3. Proteolytic cleavage of these proteins yields characteristic products which may exert regulatory effects on the translational machinery. Inhibition of caspase activity protects protein synthesis from long-term inhibition in cells treated with some, but not all, inducers of apoptosis. This review describes the initiation factor modifications and the possible signalling pathways by which translation may be regulated during apoptosis. 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| subjects | Adapter proteins Animals Apoptosis Apoptosis - genetics Apoptosis - physiology Biochemistry Caspases - metabolism Cell death Humans Kinases Peptide Biosynthesis Peptide Initiation Factors - metabolism Phosphorylation Physiology Polypeptides Protein Biosynthesis - physiology Protein Kinases - metabolism Protein synthesis Signal Transduction |
| title | Translation initiation factor modifications and the regulation of protein synthesis in apoptotic cells |
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