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DCP2 decapping enzyme homolog

Dcp2, Dcp2p
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.[provided by RefSeq, Jun 2011] (from NCBI)
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Top mentioned proteins: Dcp1, CAN, caspase-3, STEP, EDC3
Papers on Dcp2
Geminivirus Activates ASYMMETRIC LEAVES 2 to Accelerate Cytoplasmic DCP2-Mediated mRNA Turnover and Weakens RNA Silencing in Arabidopsis.
Chua et al., Singapore, Singapore. In Plos Pathog, Oct 2015
We found that AS2 promotes DCP2 decapping activity, accelerates mRNA turnover rate, inhibits siRNA accumulation and functions as an endogenous suppressor of PTGS.
Mobilization of Dormant Cnot7 mRNA Promotes Deadenylation of Maternal Transcripts During Mouse Oocyte Maturation.
Schultz et al., Philadelphia, United States. In Biol Reprod, Aug 2015
We previously demonstrated that phosphorylation of MSY2, an RNA-binding protein, and mobilization of mRNAs encoding the DCP1A-DCP2 decapping complex contribute to maternal mRNA destruction during meiotic maturation.
Mutations in DCPS and EDC3 in autosomal recessive intellectual disability indicate a crucial role for mRNA decapping in neurodevelopment.
Jamra et al., Toronto, Canada. In Hum Mol Genet, Jul 2015
EDC3 stimulates DCP2, which decaps mRNAs at the beginning of the 5' to 3' degradation pathway.
Both the autophagy and proteasomal pathways facilitate the Ubp3p-dependent depletion of a subset of translation and RNA turnover factors during nitrogen starvation in Saccharomyces cerevisiae.
Bedwell et al., Birmingham, United States. In Rna, May 2015
In contrast, the deadenylase subunit Pop2p and the decapping enzyme Dcp2p were rapidly depleted by a proteasome-dependent mechanism.
Role of cytoplasmic deadenylation and mRNA decay factors in yeast apoptosis.
N M et al., Hyderābād, India. In Fems Yeast Res, Mar 2015
Strains of Saccharomyces cerevisiae lacking factors involved in 5' to 3' mRNA decay pathway (DCP1, DCP2, DHH1, PAT1, LSM1 and LSM4) exhibit caspase-dependent apoptosis and accelerated chronological aging.
Different roles for RNA silencing and RNA processing components in virus recovery and virus-induced gene silencing in plants.
Moffett et al., Wuhan, China. In J Exp Bot, Feb 2015
Consistent with this, we found that viral recovery induced increased PB formation and that a decapping mutant (DCP2) showed increased VIGS and virus RNA accumulation, indicating an important role for PBs in eliminating viral RNA.
Diffuse decapping enzyme DCP2 accumulates in DCP1 foci under heat stress in Arabidopsis thaliana.
Watanabe et al., Tokyo, Japan. In Plant Cell Physiol, 2015
The decapping enzymes DCP1 and DCP2 are components of a decapping complex that degrades mRNAs.
Efficient preparation and properties of mRNAs containing a fluorescent cap analog: Anthraniloyl-m(7)GpppG.
Goss et al., Melbourne, Australia. In Translation (austin), 2015
The Ant-m(7)G derivative, which has been previously shown to interact with the eukaryotic cap binding protein eIF4E, is shown in this paper to be a substrate for the Vaccinia capping enzyme and the DCP2 decapping enzyme from Arabidopsis.
Quality control of assembly-defective U1 snRNAs by decapping and 5'-to-3' exonucleolytic digestion.
Parker et al., Boulder, United States. In Proc Natl Acad Sci U S A, 2014
To determine how assembly-defective snRNAs are degraded, we first demonstrate that yeast U1 Sm-mutant snRNAs are degraded either by Rrp6- or by Dcp2-dependent decapping/5'-to-3' decay.
The role of disordered protein regions in the assembly of decapping complexes and RNP granules.
Izaurralde et al., Tübingen, Germany. In Genes Dev, 2014
The removal of the 5' cap structure by the decapping enzyme DCP2 inhibits translation and generally commits the mRNA to irreversible 5'-to-3' exonucleolytic degradation by XRN1.
The 5' → 3' exoribonuclease XRN1/Pacman and its functions in cellular processes and development.
Newbury et al., Brighton, United Kingdom. In Wiley Interdiscip Rev Rna, 2012
In eukaryotic cells, XRN1 is often found in particles known as processing bodies (P bodies) together with other proteins involved in the 5' → 3' degradation pathway, such as DCP2 and the helicase DHH1 (Me31B).
Ubiquitylation of the initiator caspase DREDD is required for innate immune signalling.
Meier et al., London, United Kingdom. In Embo J, 2012
The authors show that stimulation of the Drosophila pattern recognition protein PGRP-LCx induces DIAP2-dependent polyubiquitylation of the initiator caspase DREDD.
Dcp2 decapping protein modulates mRNA stability of the critical interferon regulatory factor (IRF) IRF-7.
Kiledjian et al., United States. In Mol Cell Biol, 2012
In this study the increase in Irf-7 mRNA within the background of reduced Dcp2 levels was attributed to a stabilization of the Irf-7 mRNA, suggesting that Dcp2 normally modulates Irf-7 mRNA stability.
The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.
Sprangers et al., Tübingen, Germany. In Embo J, 2012
Edc3 & Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. Protein interactions via LSm & HLM domains were identified.
The protein Dredd is an essential component of the c-Jun N-terminal kinase pathway in the Drosophila immune response.
Foley et al., Edmonton, Canada. In J Biol Chem, 2011
Dredd is an essential component of the IMD pathway required for the full activation of IMD/dJNK in cell culture and in vivo
Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.
Gross et al., San Francisco, United States. In Rna, 2011
Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition
Advancement of global health: key messages from the Disease Control Priorities Project.
Jamison et al., Washington, D.C., United States. In Lancet, 2006
A major product of DCPP, Disease Control Priorities in Developing Countries, 2nd edition (DCP2), focuses on the assessment of the cost-effectiveness of health-improving strategies (or interventions) for the conditions responsible for the greatest burden of disease.
Surgery and Trauma Care
Spiegel et al., Washington, D.C., United States. In Unknown Journal, 0001
The chapter on surgery in the Disease Control Priorities in Developing Countries, second edition (DCP2) (Jamison and others 2006) exposed the scarcity of relevant evidence on outcomes, effectiveness, and cost-effectiveness in the literature from the developing world; unfortunately, this situation has improved only mildly.
Benefit-Cost Analysis for Selected Surgical Interventions in Low- and Middle-Income Countries
Meara et al., Washington, D.C., United States. In Unknown Journal, 0001
Since surgery was first included in the second edition of Disease Control Priorities (DCP2, 2006), research examining the cost-effectiveness of surgical interventions in low- and middle-income countries (LMICs) has expanded substantially (see chapter 18).
Essential Surgery: Key Messages of This Volume
Debas et al., Washington, D.C., United States. In Unknown Journal, 0001
By design, DCP2, published in 2006, placed much more emphasis on surgery than had previous health policy documents.
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