The mammalian target of rapamycin complex 1 (mTORC1) is involved in the cellular 
transcription and translation processes. The undertaken study characterized the 
enhancer of mRNA decapping protein 4 (Edc4) as mTORC1 interacting protein. Human 
T lymphoblast (CCRF-CEM) cells were used for mTORC1 purification. 
Co-immunoprecipitation coupled with immunoblotting analysis was used to confirm 
the interaction of Edc4 in mTORC1 specific purifications. Further assays were 
incorporated to conclude the role of mTORC1 in mRNA decapping via Edc4. Edc4 was 
identified as a new interacting protein with mTORC1 in both the endogenous and 
myc-tag raptor component mTORC1 specific purifications. Quantitative 
co-localization using confocal microscopy demonstrated that raptor component of 
mTORC1 coexists with Edc4 in processing (P) bodies, a site for mRNA degradation. 
Incubation of cells with rapamycin, a known inhibitor of mTOR kinase activity, 
increased the total Edc4 protein expression but at the same time decreased the 
Edc4 interaction with mTORC1. Moreover, rapamycin treatment resulted in a 
significant decrease in total serine phosphorylated Edc4 protein signal and the 
total 5'-capped mRNA. These findings provide the first evidence for the pivotal 
role of mTORC1 in Edc4 regulation. Further in-depth studies are required to get 
a complete understanding of molecular crosstalk between mTORC1 signaling and 
mRNA decapping pathway.