Mille viae in eukaryotic mRNA decapping. (December 2017)

• Record Type: Journal Article
• Authors: Valkov, Eugene; Jonas, Stefanie; Weichenrieder, Oliver
• Is Part Of: Current opinion in structural biology. Volume 47(2017)
• Page Start: 40
• Page End: 51
• Publication Date: 2017-12
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2017.05.009
• Languages: English
• ISSNs: 0959-440X

Abstract

Graphical abstract: Highlights: Conformations of the eukaryotic mRNA decapping complex. mRNA substrate recognition by NUDIX pyrophosphatases. Flow scheme of eukaryotic decapping factor interactions. Abstract : Cellular mRNA levels are regulated via rates of transcription and decay. Since the removal of the mRNA 5′-cap by the decapping enzyme DCP2 is generally an irreversible step towards decay, it requires regulation. Control of DCP2 activity is likely effected by two interdependent means: by conformational control of the DCP2–DCP1 complex, and by assembly control of the decapping network, an array of mutually interacting effector proteins. Here, we compare three recent and conformationally distinct crystal structures of the DCP2–DCP1 decapping complex in the presence of substrate analogs and decapping enhancers and we discuss alternative substrate recognition modes for the catalytic domain of DCP2. Together with structure-based insight into decapping network assembly, we propose that DCP2-mediated decapping follows more than one path.