Regulation of gene expression at the level of translation provides a fast response to environmental stimuli. The CCR4-Not complex is an important regulator of gene expression in eukaryotic cells. It regulates both mRNA stability and protein life span. Indeed, the Ccr4-Not complex influences the poly-A tail as well as the capacity to send proteins to the degradation pathway of the proteasome. Recent studies indicate that it also regulates translation. Many interactions of the Ccr4-Not complex to other proteins have been described some of which were interesting for this study. One of them is the interaction with Pbp1, a protein we identified in the purification of a new type of Not1 granules: the assemblysomes. Pbp1 is known to be component of glucose deprivation-induced stress granules; it is involved in P-body-dependent granule assembly; and it is the ortholog of human ataxin-2 involved in neurodegenerative diseases. Pbp1 protein in yeast is known to be interacting with Pab1, poly (A)-binding protein. Moreover, its deletion suppresses the lethal Pab1 deletion. Since it was identified in Not1-containing assemblysomes, the main goal of this study was to focus on the involvement and function of the Pbp1 in the formation and function of this new type of granules: the Not1-containing assemblysomes.