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The protein encoded by DCP2 is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD).
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ERK (show EPHB2 Proteins)-phosphorylated Dcp1a (show DCP1A Proteins) enhances its interaction with the decapping enzyme (show DCP1A Proteins) Dcp2 during early differentiation of 3T3-L1 cells.
Recruitment of DCP1A (show DCP1A Proteins) and DCP2 increases the mRNA degradation capacity of the maturing oocyte so that by the 2-cell stage, most of the maternal mRNA is degraded.
The results showed that DCP1A (show DCP1A Proteins) and DCP2 are critical in the transition from mRNA stability to instability during meiotic maturation and that mRNA degradation must be successful to execute the oocyte-to-zygote transition.
In this study the increase in Irf-7 (show IRF7 Proteins) mRNA within the background of reduced Dcp2 levels was attributed to a stabilization of the Irf-7 (show IRF7 Proteins) mRNA, suggesting that Dcp2 normally modulates Irf-7 (show IRF7 Proteins) mRNA stability.
Like Dcp2, Nudt16 (show NUDT16 Proteins) also regulates the stability of a subset of mRNAs including a member of the motin family of proteins involved in angiogenesis.
Human Dcp2 levels and activity are controlled by a competition between decapping complex assembly and Dcp2 degradation.
The data indicates that DCP2 activation by DCP1 (show ACE Proteins) occurs preferentially on the EDC4 (show EDC4 Proteins) scaffold, which may serve to couple DCP2 activation by DCP1 (show ACE Proteins) with 5'-to-3' mRNA degradation by XRN1 (show XRN1 Proteins) in human cells.
Data show that Y14 (show RBM8A Proteins) interacts directly with the decapping factor Dcp2 and the 5' cap structure of mRNAs via different but overlapping domains.
PNRC2 (show PNRC2 Proteins) acts in synergy with Dcp1a (show DCP1A Proteins) to stimulate the decapping activity of Dcp2 by bridging the interaction between Dcp1a (show DCP1A Proteins) and Dcp2.
an mRNA decapping enzyme (show DCPS Proteins) demonstrated to contain intrinsic decapping activity
Human Dcp2 is a catalytically active mRNA decapping enzyme (show DCPS Proteins) that localizes to the cytoplasm
LSm1 (show LSM1 Proteins)-7 proteins colocalize with DCP1 (show ACE Proteins),DCP2 and Xrn1 (show XRN1 Proteins) in cytoplasmic foci
These data support the novel notion of the association between Ro52 (show TRIM21 Proteins) with hDCP2 protein in cytoplasmic p-bodies, playing a role in mRNA metabolism in response to cellular stimulation.
The protein encoded by this gene is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It removes the 7-methyl guanine cap structure from mRNA, prior to its degradation from the 5' end. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.
mRNA-decapping enzyme 2
, DCP2 decapping enzyme homolog
, m7GpppN-mRNA hydrolase
, nudix (nucleoside diphosphate linked moiety X)-type motif 20