By Simon J. Morley (auth.), Professor Dr. Robert E. Rhoads (eds.)

This quantity provides the reaction of the eukaryotic translational gear to mobile pressure and apoptosis, together with kinases activated via either the ERK and stress-activated pathways. It extra explores brokers that inhibit protein synthesis, calcium and the immunosuppressant rapamycin. Six chapters written by way of top specialists within the box offer either new info and complete literature studies. either the rules of initiation and elongation are mentioned, and the mechanisms of apoptosis are regarding alterations within the protein synthesis machinery.

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Extra resources for Signaling Pathways for Translation: Stress, Calcium, and Rapamycin

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R:. Qj .. l! SA-C. Apoptosis in Jurkat T cells is associated with the inhibition of protein synthesis and cleavage of eIF4G. FMK prior to incubation with or without 250 ng/ml anti-Fas antiserum. Rates of protein synthesis were estimated by pulse-Iabelling with [35 5] methionine for 30 min before harvesting at the times indicated. B Parallel cultures were used to determine cell viability, as estimated by trypan blue exclusion, and confirmed by FACS analysis (data not shown). C Jurkat cells were incubated in the absence or presence of 250ng/ml anti-Fas antiserum for the times shown.

2000a, b). In the last case, cleavage did not affect its binding to eIF4E (Bushell et al. 2000a) and was not observed in Jurkat cells treated with anti-Fas antiserum or in the reticulocyte lysate incubated with caspase-3 (M. Bushell and S. Modey, unpubl. data). Cleavage of eIF4B and eIF3p35 occurred with delayed kinetics relative to those seen for eIF4GI, and was also observed in response to serum deprivation and treatment of cells with anti-Fas antiserum or etoposide. The cleavage of eIF4GI, the transient increase in the phosphorylation of eIF2a, and the increased association of 4E-BPI with eIF4E was also observed with other inducers of apoptosis, such as etoposide or staurosporine (S.

EIF4E and associated proteins were recovered and resolved by SDS-PAGE and immunoblotting for eIF4e and eIF4G and its cleavage fragments (using antisera W, RL and E), as indicated (right panel). (Data from Bushell et al. 2000a) .. n X 4EA I I 3/4/\ T~-~-~_n __ Ar C-3 N & (1) v f; n p.. ~ ~ & ~ Cl f; n C1

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