The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1

摘要: The removal of the 5′-cap structure by decapping enzyme DCP2 and its coactivator DCP1 shuts down translation exposes mRNA to 5′-to-3′ exonucleolytic degradation XRN1. Although yeast directly interact, an additional factor, EDC4, promotes DCP1–DCP2 association in metazoan. Here, we elucidate how human proteins interact assemble active complex decapped mRNAs are handed over We show that EDC4 serves as a scaffold for assembly, providing binding sites DCP1, XRN1 bind simultaneously C-terminal domain through short linear motifs (SLiMs). Additionally, form direct but weak interactions facilitated EDC4. Mutational functional studies indicate docking on is critical step vivo. They also revealed crucial role conserved asparagine–arginine containing loop (the NR-loop) EVH1 activation. Our data activation occurs preferentially scaffold, which may serve couple with cells.