Different transcription factors bind on the promoter region will trigger the downstream translation processes.
eIF2 α phosphorylation also triggers the specific translation of activating transcription factor 4 (ATF4), which is essential for the upregulation of different foldases and the regulation of the redox and metabolic status of the cell.
It is required for the activity of GCN2, which triggers the preferential translation of mRNA encoding the GCN4 transcription factor, which controls the expression of genes encoding proteins involved in amino-acid biosynthesis [ 45].
Interestingly, like the AA starvation sensor, GCN2, PKR similarly triggers phosphorylation of the translation regulator eIF2α, thus resulting in translation regulation under stress (Dauber and Wolff, 2009).
SraL targets the ribosome-associated protein folding chaperone, trigger factor, via binding to the translation initiation region of tig mRNA [ 32].
Critically, it is precisely this function that must have triggered the evolution of the translation machinery.
The first possibility is that the translation arrest is triggered as part of a general stress response, perhaps as a consequence of lack of VSG synthesis or deposition on the cell surface.
Finally, while no disease examples have been documented thus far, it is plausible that reserve systems able to compensate for defects in the translation pathway are triggered in specific cell types, sparing them from deleterious effects.
Investigation of the mechanisms that trigger local translation revealed a role for calcium-dependent retrograde netrin-1/DCC receptor signaling.
The first, GCVT, is selectively triggered by glycine [ 45] and controls the translation of the aminomethyltransferase mRNA (BP0195).
