Expression profiles and ICG-001 Wnt/beta-catenin inhibitor adaptation to changed environmental conditions, when the Bortezomib translation of certain transcripts is inhibited and, on the other hand, the translation of new transcripts is induced. They are present in cells even under non-stress conditions and they enlarge under various stresses, such as a heat shock at 39uC and 42uC. However, one of the major components of Pbodies, Dcp2p that is engaged in mRNA decapping, is also a component of the robust heat shock-induced SGs, which may form independently of the P-bodies scaffolding proteins Edc3 and Lsm4. On the contrary to glucose-deprived cells and cells heat-shocked at 37uC, we show here that Dcp2 foci formed in cells heat-shocked at 42uC do not depend on these scaffolds. These Dcp2 accumulations do not contain translation initiation factors and still serve as sites for assembly of SGs upon continuous and more robust heat stress. They might be considered as “premature SGs”, as well as Dcp2-containing structures related to P-bodies. The stress-induced phosphorylation of translation initiation factor eIF2a is the best characterized mechanism of stress granule assembly. However, there are other ways, how to induce SGs or influence their dynamics. Apart influencing other translation initiation factors, they concern the metabolism of polyamines or hexosamines and the stress-induced tRNA derivates. Moreover, since eIF2a-phosphorylation independent mechanisms of SGs assembly prevail in lower eukaryotes, it seems that these are evolutionary older. We show here that accumulations of translation elongation factor eEF3 on Dcp2 foci at 42uC precede assembly of eIF3-containing SGs in cells heat-shocked at 46uC. This suggests that the translation elongation phase is affected first in the stressed cells. It is conceivable that there might be a shortage of the eEF3 factor due to its sequestration into cytoplasmic foci at 42uC. This may cause an alteration of kinetics of the translation elongation, which results in a deceleration of translation initiation. Such regulation of translation at the elongation step has also been proposed as a possible function of the Stm1 protein, which is able to stall ribosomes after the 80S complex formation in vitro and to promote decapping of a subset of mRNA. Moreover, Stm1p has been shown to regulate interaction of eEF3 factor with ribosomes and to play a complementary role to eEF3 in translation under nutrient stress conditions. Interestingly, we did not observe an accumulation of Stm1-GFP fusion protein neither upon heat shock at 42uC nor under heat shock at 46uC. Additionally, we did not see any effect of the stm1D on assembly of SGs in cells heat-shocked at 46uC. Therefore, the roles of Stm1 protein and eEF3 factor in the Gcn2-independent signaling and translation repression resulting in SGs assembly in heat-shocked cells remain elusive. Meanwhile assembly of P-bodies is generally connected with reprogramming of cells to new growth conditions, SGs are formed in response to severe stresses when the translation of housekeeping genes is completely shut down. Although SGs are thought to be sites where mRNA molecules are sorted, selected, and together with translation factors, sheltered from the effects of a stress, the fate of SGs components after a stress relief is mainly unknown. However, it is conceivable that at least some SGs protein components may also return back to the active translation.