mRNA-decapping enzyme 2 (DCP2)

mRNA-decapping enzyme 2 (DCP2) is the primary eukaryotic enzyme that removes the protective 5' cap (m⁷GpppN) from mRNA, which is a critical step in initiating 5' to 3' mRNA decay. DCP2 contains an N-terminal regulatory domain, a catalytic domain with a signature NUDIX motif responsible for hydrolyzing the cap structure, and an intrinsically disordered C-terminal region. DCP2 is activated by cofactors such as DCP1, Edc1, and Edc3, and works as part of large multiprotein complexes, often localized in cytoplasmic processing bodies (P-bodies). DCP2 recognizes capped RNA substrates and, through its NUDIX domain, releases 7-methylguanosine diphosphate (m⁷GDP) and a 5'-monophosphorylated mRNA, which is then degraded by exonucleases[1][2][3][4][5]. Dysregulation of DCP2 or its cofactors can impact mRNA stability and homeostasis, influencing cellular gene expression and potentially contributing to diseases such as cancer through the misregulation of transcript decay.

Other names

m7GpppN-mRNA hydrolaseDCP2NUDT20Nudix motif 20hDpcNucleoside diphosphate-linked moiety X motif 20nudix (nucleoside diphosphate linked moiety X)-type motif 20DCP2 decapping enzyme homologmRNA-decapping enzyme 2

Hydrolysis of the 5' mRNA cap structure (decapping), enabling mRNA decay