Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures

By E. van Dijk, Nicolas Cougot, S. Meyer, S. Babajko, E. Wahle, Bertrand Séraphin. 2002

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In Molecular Biology

Citations in the corpus

The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands (2022, background): “Abundant cellular p1dsRNAs also include mRNA degradation and triphosphorylase intermediates (Braun et al., 2012; Choi et al., 2020; Choi and Sullivan, 2021; Jonas and Izaurralde, 2013; Nagarajan et al., 2013; van Dijk et al., 2002).”
P bodies and the control of mRNA translation and degradation. (2007, background): “For example, some members of the Puf family of proteins in humans and yeast bind 3 0 UTRs in a sequence-specific manner and directly interact with the Pop2p subunit of the Ccr4/Pop2/Not complex, thereby recruiting the Fly (Behm-Ansmant et al., 2006) Human (van Dijk et al., 2002; Ingelfinger et al., ”
P-Body Formation Is a Consequence, Not the Cause, of RNA-Mediated Gene Silencing (2007, result): “The size of Drosophila P bodies also depends on the fraction of mRNAs undergoing decapping, in agreement with the results reported for yeast and human cells (4, 14, 16, 25, 44, 48, 53).”
General translational repression by activators of mRNA decapping. (2005, background): “, the decapping machinery (Bashkirov et al., 1997; Ingelfinger et al., 2002; Lykke-Andersen, 2002; Van Dijk et al., 2002; Teixeira et al., 2005), and are sites where decapping can occur (Sheth and Parker, 2003; Cougot et al., 2004).”
The enzymes and control of eukaryotic mRNA turnover (2004, background): “Hydrolysis of the cap structure by Dcp1p–Dcp2p, or by Dcp2p alone, releases m 7 GD”
mRNA capping: biological functions and applications (2016, unknown): “Eukaryotic cells maintain a cytoplasmic pool of uncapped mRNA in the form of messenger ribonucleo-protein (mRNP) in the P-bodies, where storage, deadenylation and decapping of the mRNA can take place (20–22).”
Cytoplasmic foci are sites of mRNA decay in human cells (2004, methodology): “To test this hypothesis, we transiently transfected HEK293 cells with GFP fusions and assayed simultaneously for the localization of endogenous hDcp1a by indirect immunofluorescence using a rabbit serum ( van Dijk et al., 2002 ) and anti‐rabbit IgG coupled to Cy5 as a secondary antibody.”
Mammalian stress granules and processing bodies. (2007, background): “Mammalian PBs (also known as GWBs [Eystathioy et al., 2002, 2003] or DCP foci [Ingelfinger et al., 2002; van Dijk et al., 2002 ], contain components of the 50 to 30 decay machinery (Xrn1, DCP1/DCP2,”
Processing bodies require RNA for assembly and contain nontranslating mRNAs. (2005, background): “…(Dcp1p/Dcp2p), activators of decapping, Dhh1p (referred to as RCK in mammals), Pat1p, Lsm1–7p, Edc3p, and the 5 –3 exonuclease Xrn1p (Bashkirov et al. 1997; Ingelfinger et al. 2002; Lykke-Andersen 2002; van Dijk et al. 2002; Sheth and Parker 2003; Cougot et al. 2004; Kshirsagar and Parker 2004).”
MicroRNA: Biogenesis, Function and Role in Cancer (2010, background): “Translation occurs in three stages: initiation, elongation and termination, which require coordination of multiple protein factors [186].”
The role of disordered protein regions in the assembly of decapping complexes and RNP granules (2013, background): “…DCP2 form the conserved catalytic core of the decapping complex The decapping enzyme DCP2 belongs to the Nudix family of pyrophosphatases and catalyzes hydrolysis of the cap structure, releasing m7GDP and a 59 monophosphorylated mRNA (Lykke-Andersen 2002; van Dijk et al. 2002; Wang et al. 2002).”