Germ cells feature specialized structures known as germ granules. These granules serve as key regulation sites for gene expression, including translational regulation of mRNAs. Among the many proteins that localize to germ granules is the eIF4E-binding protein IFET-1. The IFET-1 RNA-protein complex includes CGH-1 (DDX6), CAR-1 (LSM14), and PATR-1(PAT-1) and determines the fates of mRNAs during the different stages of development by inhibiting the cap-dependent translation pathway. The IFET-1 RNA-protein complex is evolutionarily conserved and, in C. elegans, is localized to P-bodies associated with perinuclear P granules in germ cells. However, GFP-IFET-1, which lacks the C-terminal prion-like intrinsically disordered region (IDR) (IFET-1(-IDR)), is diffusely present through the gonad and somatic early embryonic cells. Interestingly, IFET-1(-IDR) does not rescue ifet-1(tm2944) null mutant, while the full-length GFP::IFET-1 does. This implies that IFET-1 localization to perinuclear P-bodies is required for its function. We identified IFET-1 interacting proteins by immunoprecipitating GFP-IFET-1 and GFP::IFET-1(-IDR) combined with mass spectrometry (IP-MS). Essentially, the same interaction protein cohort in both backgrounds, indicating that P-body localization is not essential for its protein interaction network. Surprisingly, GFP-IFET-1 and GFP::IFET-1(-IDR) were associated with only one of the five eIF4E isoforms, IFE-3. IFE-3 has a binding preference for the 7-methylguanosine cap on the 5’ on the mRNAs, suggesting that IFET-1 may translationally repress specific mRNAs based on the 5’ cap chemistry. We hypothesize that the IDR of IFET-1 is critical for liquid-liquid phase separation (LLPS), which drives its P-body localization and the binding and repression of specific mRNA targets. The IFET-1 complex is an ideal model for understanding LLPS's role in RNA-protein complex formation.