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J. Biol. Chem., Vol. 266, Issue 24, 15663-15669, 08, 1991
P Jedlicka and R Panniers
The pronounced stimulation of protein synthesis in T lymphocytes in
response to mitogens is partly due to increased cell size and hence
ribosome number. There is also a large increase in translation rate per
ribosome as a result of an increased rate of initiation. In response to
mitogen, levels of both eukaryotic initiation factor (eIF)-2 and guanine
nucleotide exchange factor, GEF, increase in parallel with ribosomes which
is consistent with a general increase in the translational machinery but
cannot explain the increase in activity per ribosome. However, as total
eIF-2 accumulates, the ratio of phosphorylated eIF-2 alpha (eIF-2(alpha P]
to eIF-2 alpha decreases. Further, the levels of eIF-2(alpha P) and GEF in
resting T lymphocytes are similar. As eIF-2(alpha P) inhibits GEF by
effectively sequestering the exchange factor in an inactive 1:1 complex,
the level of GEF available for protein synthesis initiation must be very
low in resting cells. Hence, as GEF is synthesized and rises above the
level of eIF- 2(alpha P), there will be a disproportionate increase in GEF
available for initiation compared with the increase in total GEF. This
increase in available GEF is probably great enough to support the increase
in translation rate per ribosome as well as the increase in ribosome
number.
Mechanism of activation of protein synthesis initiation in mitogen- stimulated T lymphocytes
University of Rochester Cancer Center, New York.
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