DCP2 is a decapping metalloenzyme that catalyzes removal of the 7-methylguanine cap structure from mRNAs, producing 5'-phosphorylated mRNA and 7m-GDP 1. This catalytic activity is essential for mRNA degradation pathways, including normal mRNA turnover and nonsense-mediated decay 2. DCP2 shows preferential activity toward deadenylated mRNAs 3 and is recruited to processing bodies (P-bodies) where it functions within mRNA decay complexes scaffolded by EDC4 and coupled with 5'-3' exonuclease XRN1 4. DCP2 activity is enhanced by multiple regulatory proteins, particularly DCP1, which increases mRNA-binding affinity through its EVH1 domain 5. N(6)-methyladenosine modifications (m6A) at the cap position confer resistance to DCP2-mediated decapping 6, providing a regulatory mechanism for selective mRNA protection. Beyond standard mRNA decay, DCP2 participates in specialized processes including histone mRNA degradation 7 and LINE-1 retrotransposon silencing through MOV10-mediated recruitment 8. DCP2 levels are controlled by competition between complex assembly with Hedls and proteasomal degradation 9. Clinically, DCP2 expression correlates with chemoresistance in small cell lung cancer through m6A-mediated regulation 10, suggesting therapeutic potential for modulating DCP2 function in cancer treatment.