DCP2 is a metalloenzyme that catalyzes removal of the 7-methylguanine cap structure from mRNAs, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. This decapping activity is essential for mRNA degradation pathways, including normal mRNA turnover, nonsense-mediated decay, and replication-dependent histone mRNA degradation. DCP2 shows higher activity toward deadenylated mRNAs and is inhibited when mRNAs carry N(6)-methyladenosine modifications at the cap (m6A(m)), which provides resistance to decapping 1. The enzyme is recruited to processing bodies through interactions with scaffolding proteins such as EDC4, where it coordinates with the 5'–3' exonuclease XRN1 to link decapping with decay 2. DCP2 activity is dynamically controlled by binding to activators including DCP1 and Hedls; notably, in the absence of Hedls, DCP2 is targeted for proteasomal degradation, restricting accumulation of uncomplexed enzyme 3. Beyond canonical mRNA decay, DCP2 participates in LINE-1 retrotransposon silencing through phase-separated complexes with MOV10 4 and blocks autophagy during nutrient-rich conditions by degrading ATG-related transcripts. Recent studies in small cell lung cancer indicate that m6A-mediated DCP2 degradation promotes mitophagy and chemotherapy resistance, suggesting DCP2 as a potential therapeutic target in this context 5.