Translation inhibition occurs in response to stress, when other cellular activities have to be reassigned or suspended momentarily. We demonstrate here that the activation of PKR by cytosolic dsRNA results in a stress response, leading to ATF4 and GADD34 induction. GADD34 expression has been observed during the infection of cells by different types of viruses [62] or intracellular bacteria such as Listeria monocytogenes [63] . Our observations demonstrate that GADD34 expression is a direct consequence of PKR activation and dsRNA sensing. Interestingly, although GADD34 induction by poly I:C promotes eIF2a dephosphorylation, this is not sufficient to prevent global protein synthesis arrest. The uncoupling of efficient eIF2a dephosphorylation from global translation recovery in response to cytosolic poly I:C implies therefore the existence of additional mechanisms inhibiting global translation. The 2-5A/RNAse L pathway does not seem to be sufficiently active in our experimental setting to explain this prolonged protein synthesis inhibition. The cleavage or the inactivation of other translation factors could work in concert with eIF2a to block or affect the efficiency of other individual steps of mRNA translation [64] . For instance, the phosphorylation of translation elongation factor 2 (eEF-2) is also controlled by eIF2a phosphorylation. Thus, Thr56 phosphorylation of eEF-2, which is known to inhibit its translational function by reducing its affinity for ribosomes, could contribute directly to the protein synthesis inhibition induced by PKR activation [65] . Independently of general protein synthesis inhibition, eIF2a dephosphorylation is necessary for the production of specific proteins upon dsRNA-induced translation inhibition. As demonstrated for ATF4, translation of a given mRNA during stress could rely on the structure and organization of its coding sequence, as well as the presence of multiple alternative initiation codons [49] . Surprisingly, functional GADD34 expression was found necessary for the translation of IL-6, IFN-b, and PKR. This observation points to the existence of a distinct group of mRNAs efficiently translated upon dsRNA detection and dependent on GADD34 activity. GADD34 is extremely short lived and has been shown to accumulate on the ER, when over-expressed [51] . GADD34 could mediate its activity at the ER level and influence differently eIF2a sub-cellular distribution according to the type, localization, and level of activity displayed by the different eIF2a kinases. The strong eIF2a phosphorylation mediated by PKR in response to poly I:C or viral infection and leading to the initiation of translation inhibition, could be circumvented through GADD34 activity solely at the ER level, thereby allowing local cytokine production in absence of other functional protein synthesis. This selectivity for translation of several specific mRNAs among other ER-secreted molecules suggests further that GADD34 dependent mRNAs might display specific features allowing their efficient identification by GADD34 and associated molecules, as well as allowing their translation in presence of minimal levels of active guanine nucleotide exchange factor eIF2B.