DDX6 is a DEAD-box RNA helicase essential for P-body assembly and function, serving as a critical regulator of mRNA metabolism and cellular stress responses. Structurally, DDX6 contains an FDF motif in its RecA2 domain that mediates ribosome interactions 1, and its functions require both ATPase activity and RNA-binding capacity 1. Mechanistically, DDX6 coordinates mRNA storage in P-bodies, cytoplasmic ribonucleoprotein granules where translationally inactive mRNAs are sequestered to prevent degradation 23. DDX6 participates in mRNA decapping and deadenylation-dependent decay of inefficiently translated mRNAs, with helicase activity required for proper separation of P-bodies from stress granules 45. During phase separation, DDX6 assembles P-bodies that function as mRNA reservoirs, protecting transcripts like BCAT1 from degradation 6. DDX6 also limits stress granule formation through its RNA chaperone activity and modulates NLRP3 inflammasome assembly via interactions with p62 78. Disease relevance includes intellectual developmental disorder with impaired language and dysmorphic facies. Clinically, DDX6 represents a therapeutic vulnerability in acute myeloid leukemia, where inhibition sensitizes cells to chemotherapy by depleting metabolic mRNAs 6.