Affinage

DCP1A

mRNA-decapping enzyme 1A · UniProt Q9NPI6

Length
582 aa
Mass
63.3 kDa
Annotated
2026-06-09
29 papers in source corpus 19 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DCP1A is a cofactor of the mRNA cap hydrolase DCP2 that nucleates cytoplasmic P bodies and couples mRNA decapping and decay to cell-state transitions, antiviral defense, and TGFβ-dependent transcription (PMID:39256052, PMID:21859862, PMID:11836524). Within the decapping machinery, its N-terminal EVH1 domain mediates the strongest interaction with DCP2, while its proline-rich C-terminal extension engages Ddx6 and Edc3 (PMID:23637887); DCP1A and the paralog DCP1B act non-redundantly, with DCP1A required for decapping-complex assembly and contacts with cap-binding proteins and DCP1B linking to degradation and translational machinery, such that each governs turnover of distinct mRNA sets (PMID:39256052). DCP1A activity and P body dynamics are set by phosphorylation through multiple kinases: JNK phosphorylates Ser315 and sustained activation disperses DCP1A from P bodies and stabilizes IL-8 mRNA (PMID:21859862), ERK drives dual Ser315/Ser319 phosphorylation that enhances DCP1A–DCP2 association (PMID:23637887), mitotic hyperphosphorylation at Ser315 accompanies P body disassembly during division (PMID:23300942), and MEK1 phosphorylation of Ser563 antagonizes P body formation and RNA storage to control embryonic stem cell self-renewal and differentiation (PMID:39671288). DCP1A protein levels are additionally limited by malin-mediated ubiquitin–proteasome degradation, which tunes microRNA silencing (PMID:23131811). Through this decapping function DCP1A drives developmental and physiological mRNA clearance: it is essential for mouse embryonic growth and cardiac development (PMID:33813271), mediates maternal mRNA degradation during oocyte maturation and postovulatory aging (PMID:23136299, PMID:38001238, PMID:39629683), and regulates muscle satellite cell proliferation and differentiation (PMID:34238354). Independently, DCP1A (SMIF) functions as a Smad4-specific transcriptional co-activator that translocates to the nucleus upon TGFβ/BMP4 signaling and requires p300/CBP for activity (PMID:11836524). DCP1A is also an interferon-stimulated gene with broad antiviral activity that is neutralized by viral 3C-like proteases, which cleave it at Q343 (or E238 in porcine DCP1A), with cleavage-resistant mutants retaining enhanced antiviral function (PMID:30158128, PMID:32461317, PMID:36758802, PMID:37283741, PMID:40022242).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2002 High

    Established a transcriptional, signaling role for DCP1A before its decapping function was known, showing it acts as a Smad4-specific nuclear co-activator in TGFβ/BMP4 signaling.

    Evidence Co-IP, transcriptional reporter assays, Smad4 point mutant, and zebrafish morpholino knockdown

    PMID:11836524

    Open questions at the time
    • Does not connect the nuclear co-activator role to DCP1A's cytoplasmic decapping function
    • Mechanism of nuclear/cytoplasmic partitioning not resolved
  2. 2008 Low

    First indicated that DCP1A phosphorylation is a regulated event tied to neuronal development and stress, raising the question of which kinases and sites are involved.

    Evidence Phosphorylation analysis across neuronal development and stress with residue identification

    PMID:19084008

    Open questions at the time
    • Limited methodological detail and no rigorously established functional consequence
    • Responsible kinases not identified
  3. 2011 High

    Identified JNK as a kinase that phosphorylates DCP1A at Ser315, linking stress kinase signaling to P body dynamics and mRNA stability.

    Evidence In vitro kinase assay, Co-IP, live-cell imaging, S315 phosphomimetic mutagenesis with IL-8 mRNA readout

    PMID:21859862

    Open questions at the time
    • Mechanism linking DCP1A overexpression to NF-κB suppression not fully resolved
    • Whether dispersion reflects loss of decapping activity not tested directly
  4. 2013 High

    Mapped DCP1A's modular interactions and showed ERK-driven dual Ser315/Ser319 phosphorylation selectively strengthens DCP1A–DCP2 binding, defining how signaling tunes decapping-complex composition.

    Evidence Co-IP, mass spectrometry, site-directed mutagenesis, kinase assay, phosphomimetic pulldown

    PMID:23637887

    Open questions at the time
    • Effect on decapping catalytic output not quantified
    • Interplay between ERK and JNK phosphorylation not resolved
  5. 2013 Medium

    Connected DCP1A phosphorylation to the cell cycle, showing mitotic hyperphosphorylation (Ser315-dependent) accompanies P body disassembly and reassembly.

    Evidence Live-cell imaging, mitotic extract electrophoresis, truncation and mutational analysis

    PMID:23300942

    Open questions at the time
    • Mitotic kinase not definitively identified
    • Functional consequence of mitotic P body disassembly for mRNA fate unclear
  6. 2013 Medium

    Demonstrated a physiological decay role in reproduction, with DCP1A/DCP2 driving maternal mRNA degradation and zygotic genome activation during oocyte maturation.

    Evidence RNAi, morpholino knockdown, mRNA stability assays, kinase inhibitor experiments

    PMID:23136299

    Open questions at the time
    • Direct kinase responsible for DCP1A phosphorylation during maturation not confirmed
    • Target mRNA specificity not defined
  7. 2013 Medium

    Revealed a translation-control activity distinct from decapping, showing the DCP1A EVH1 domain activates PKR to phosphorylate eIF2α and arrest translation.

    Evidence GFP-Dcp1a domain mutants, eIF2α phosphorylation and PKR activation assays, poliovirus model

    PMID:24382890

    Open questions at the time
    • Mechanism by which EVH1 engages PKR unresolved
    • Relationship to canonical decapping activity unclear
  8. 2012 Medium

    Established that DCP1A protein abundance is controlled by ubiquitin-proteasome turnover via the malin E3 ligase, linking DCP1A levels to microRNA silencing.

    Evidence Co-localization, proteasome inhibition, malin depletion with DCP1A level and miRNA silencing assays

    PMID:23131811

    Open questions at the time
    • Ubiquitination sites on DCP1A not mapped
    • Signals controlling malin recruitment to P bodies unknown
  9. 2018 High

    Defined DCP1A as an interferon-stimulated antiviral effector that viral proteases neutralize, showing PRRSV nsp4 cleaves porcine DCP1A at E238 to abrogate antiviral activity.

    Evidence Overexpression, knockdown, protease cleavage assay, E238A mutagenesis, viral infection assays

    PMID:30158128

    Open questions at the time
    • Molecular basis of DCP1A antiviral restriction not defined
    • Whether antiviral function requires decapping activity untested
  10. 2020 High

    Identified Q343 as a conserved cleavage site exploited by coronavirus 3C-like proteases, generalizing the protease-counteraction strategy across CoVs.

    Evidence Protease cleavage assay, Q343A mutagenesis, viral infection assays, sequence conservation analysis

    PMID:32461317

    Open questions at the time
    • Downstream antiviral effector mechanism not yet defined
    • Fragment fates after cleavage unclear
  11. 2021 High

    Established DCP1A as essential in vivo, with knockout causing embryonic lethality and cardiac defects rescued by human DCP1A.

    Evidence CRISPR/Cas9 knockout, transgenic rescue, embryonic phenotyping in mice

    PMID:33813271

    Open questions at the time
    • Molecular cause of cardiac defect not defined
    • Which DCP1A activity (decapping vs. transcriptional) underlies essentiality unknown
  12. 2021 Medium

    Showed DCP1A controls muscle satellite cell fate, with puncta appearing on activation and knockdown shifting proliferation versus differentiation and altering mRNP granule cross-regulation.

    Evidence Single myofiber isolation, live-cell imaging, polysome profiling, siRNA knockdown with proliferation/differentiation assays

    PMID:34238354

    Open questions at the time
    • Target mRNAs driving the phenotype not identified
    • Mechanism of Fmrp granule cross-regulation unresolved
  13. 2023 High

    Confirmed Q343 cleavage by SARS-CoV-2 Mpro and across coronavirus genera abolishes DCP1A ISG effector activity, strengthening DCP1A as a pan-coronavirus antiviral target.

    Evidence Protease cleavage assay, site-directed mutagenesis, ISG reporter assays in two mammalian cell lines

    PMID:36758802

    Open questions at the time
    • Effector pathway of ISG activity not mechanistically defined here
    • Alphacoronavirus weaker cleavage basis unexplained
  14. 2023 High

    Linked DCP1A cleavage to suppression of innate immune signaling, showing SADS-CoV nsp5 cleavage at Q343 inhibits IRF3/NF-κB and reduces IFN-β and cytokine output.

    Evidence Protease cleavage assay, nsp5 active-site mutagenesis, DCP1A-Q343A mutant, IFN-β and cytokine assays

    PMID:37283741

    Open questions at the time
    • Direct molecular connection between DCP1A and IRF3/NF-κB unresolved
    • Whether intact DCP1A acts upstream or as scaffold not defined
  15. 2023 Medium

    Identified DCP1A as a driver of premature maternal mRNA degradation in postovulatory oocyte aging, regulated at the level of DCP1A mRNA polyadenylation.

    Evidence Proteomics, RNA-seq, oocyte mRNA injection/siRNA, polyadenylation assays in mouse and human oocytes

    PMID:38001238

    Open questions at the time
    • Polyadenylation machinery acting on DCP1A mRNA not identified
    • Target maternal transcript specificity not defined
  16. 2024 Medium

    Confirmed DCP1A dose directly sets maternal mRNA decay rate in oocytes via gain- and loss-of-function, cementing its causal role in postovulatory aging.

    Evidence mRNA microinjection and siRNA knockdown in oocytes with RNA-seq and proteomics

    PMID:39629683

    Open questions at the time
    • Upstream regulators of DCP1A in aged oocytes not defined
    • Selectivity of degraded transcripts unresolved
  17. 2024 Medium

    Resolved DCP1A and DCP1B as non-redundant DCP2 cofactors with distinct interaction partners and distinct target mRNA repertoires, refining the architecture of the decapping complex.

    Evidence Knockdown/knockout functional dissection, Co-IP of decapping components, mRNA turnover profiling

    PMID:39256052

    Open questions at the time
    • Structural basis of paralog-specific interactions not determined
    • Single-lab; reciprocal validation of partner specificity limited
  18. 2024 High

    Defined MEK1-dependent Ser563 phosphorylation as a switch governing P body formation and RNA storage in embryonic stem cell self-renewal and differentiation.

    Evidence Quantitative phosphoproteomics, in vitro kinase assay, S563 mutagenesis, P body imaging, ESC assays

    PMID:39671288

    Open questions at the time
    • Stored mRNA targets governing ESC fate not identified
    • Integration with ERK/JNK phosphorylation inputs unresolved
  19. 2025 Medium

    Extended the antiviral mechanism by showing intact DCP1A targets viral RdRp for OPTN-mediated autophagic degradation, an activity destroyed by Q343 cleavage.

    Evidence Protease cleavage assay, Q343A mutagenesis, viral infection assay, autophagy pathway analysis

    PMID:40022242

    Open questions at the time
    • Single lab; OPTN-DCP1A interaction not reciprocally validated
    • Whether this mechanism generalizes beyond SVV unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how DCP1A's distinct activities—decapping cofactor, Smad4 transcriptional co-activator, PKR/translation regulator, and antiviral effector—are mechanistically partitioned, and which underlies its essential developmental role.
  • No structural model integrating EVH1, proline-rich, and phosphosite regions with each function
  • No unified account of nuclear vs. cytoplasmic vs. condensate DCP1A pools
  • Decapping-independence of antiviral and transcriptional roles not directly tested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 2 GO:0140098 catalytic activity, acting on RNA 1 GO:0140110 transcription regulator activity 1
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 1
Pathway
R-HSA-168256 Immune System 4 R-HSA-1266738 Developmental Biology 2 R-HSA-8953854 Metabolism of RNA 2 R-HSA-162582 Signal Transduction 1
Complex memberships
DCP2 decapping complexP bodySmad4 transcriptional complex

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 DCP1A (SMIF) was identified as a Smad4-interacting transcriptional co-activator that forms a TGFβ/BMP4-inducible complex specifically with Smad4 (not other Smads), translocates to the nucleus in a TGFβ/BMP4-inducible and Smad4-dependent manner, and requires p300/CBP for its transcriptional activity. A point mutation in Smad4 abolished binding to DCP1A and impaired transcriptional activity. Co-immunoprecipitation, transcriptional reporter assays, dominant-negative mutant overexpression, morpholino knockdown in zebrafish Nature cell biology High 11836524
2011 JNK phosphorylates DCP1A at serine 315 in vivo and in vitro, coimmunoprecipitates and colocalizes with DCP1A in P bodies, and sustained JNK activation leads to DCP1A dispersion from P bodies. Phosphomimetic mutation S315 stabilized IL-8 mRNA. Overexpressed DCP1A blocked IL-8 transcription and suppressed p65 NF-κB nuclear activity. In vitro kinase assay, co-immunoprecipitation, live-cell imaging, phosphomimetic mutagenesis, transcriptome analysis The Journal of cell biology High 21859862
2013 DCP1A interacts with Ddx6 and Edc3 through its proline-rich C-terminal extension, while its N-terminal EVH1 domain shows stronger interaction with Dcp2. ERK pathway mediates dual phosphorylation of Dcp1a at Ser315 and Ser319; phosphorylated Dcp1a enhances its interaction with Dcp2 without affecting interactions with Ddx6, Edc3, or Edc4. Co-immunoprecipitation, mass spectrometry, site-directed mutagenesis, kinase assay, phosphomimetic mutant pulldown PloS one High 23637887
2013 DCP1A is hyper-phosphorylated during mitosis; P bodies disassemble as cells prepare for division and reassemble during cytokinesis. Serine 315 is critical for hyper-phosphorylation, and serine mutations in other regions affect the dynamics of DCP1A association with P bodies as shown by live-cell imaging. Live-cell imaging, electrophoresis of mitotic cell extracts, truncation and mutational analysis, phosphorylation assays PloS one Medium 23300942
2013 DCP1A and DCP2 are encoded by maternal mRNAs that are recruited for translation during oocyte maturation via cytoplasmic polyadenylation elements. Both proteins are phosphorylated during maturation (CDC2A likely responsible, MAPK may contribute to DCP1A phosphorylation). Inhibiting DCP1A and DCP2 accumulation by RNAi or morpholinos decreased maternal mRNA degradation during meiotic maturation and reduced zygotic genome transcription. RNA interference, morpholino knockdown, mRNA stability assays, kinase inhibitor experiments Biology of reproduction Medium 23136299
2013 DCP1A expression of its N-terminal EVH1 domain is required for activation of PKR, which leads to phosphorylation of eIF2α and translational inhibition. This DCP1A-induced translational arrest is specific to DCP1A, as expression of other P-body components (Pan2, Pan3, Ccr4, Caf1) did not induce eIF2α phosphorylation. GFP-Dcp1a domain mutant expression, eIF2α phosphorylation assays, PKR activation assays, poliovirus infection model The Journal of biological chemistry Medium 24382890
2008 Dcp1a is hyperphosphorylated during brain development, neuronal differentiation, and cellular stress; specific amino acid residues responsible for phosphorylation were identified. Phosphorylation analysis during neuronal development and stress conditions, residue identification FEBS letters Low 19084008
2012 Malin E3 ubiquitin ligase is recruited to P bodies and promotes DCP1A degradation via the ubiquitin–proteasome system. Depletion of malin results in elevated DCP1A levels and altered microRNA-mediated gene silencing activity. Co-localization, ubiquitin-proteasome inhibitor experiments, malin depletion with DCP1A protein level measurement, miRNA silencing assays RNA biology Medium 23131811
2018 PRRSV nonstructural protein 4 (nsp4), a 3C-like proteinase, cleaves porcine DCP1A at glutamic acid 238 (E238), and the two cleavage products lose anti-PRRSV activity. The cleavage-resistant mutant pDCP1A-E238A retains higher antiviral activity than wild-type, establishing DCP1A as an interferon-stimulated gene with antiviral function that is targeted by viral protease. Overexpression, knockdown, protease cleavage assay, site-directed mutagenesis (E238A), viral infection assays Journal of immunology High 30158128
2020 PDCoV nsp5 (3C-like protease) cleaves DCP1A at glutamine 343 (Q343); the cleaved fragments DCP1A1-343 and DCP1A344-580 are unable to inhibit PDCoV infection. The cleavage-resistant mutant DCP1A-Q343A exhibits stronger antiviral activity. The Q343 cleavage site is conserved in mammalian DCP1A homologs, and nsp5 from seven other CoVs also cleaved DCP1A. Protease cleavage assay, site-directed mutagenesis (Q343A), viral infection assays, sequence conservation analysis Journal of virology High 32461317
2023 SARS-CoV-2 main protease (Mpro) cleaves DCP1A at residue Q343, abolishing its ISG effector activity. Mpro from multiple coronavirus genera also cleaves DCP1A, though alphacoronavirus Mpro shows weaker activity. Protease cleavage assay, site-directed mutagenesis, ISG reporter assays in mammalian cell lines The Journal of biological chemistry High 36758802
2023 SADS-CoV nsp5 cleaves DCP1A via its protease activity (requiring H41 and C144 residues); DCP1A-Q343A mutant resists cleavage and shows stronger ability to inhibit SADS-CoV infection. DCP1A cleavage by nsp5 inhibits IRF3 and NF-κB signaling pathways to decrease IFN-β and inflammatory cytokine production. Protease cleavage assay, active-site mutagenesis of nsp5 (H41, C144), DCP1A Q343A mutant, viral infection assays, IFN-β and cytokine production assays Frontiers in immunology High 37283741
2024 MEK1 phosphorylates DCP1A at S563; dephosphorylation of S563 promotes P body formation and RNA storage, facilitating both self-renewal and differentiation of mouse embryonic stem cells. DCP1A, along with P body components EDC4 and DCP2, is required for ESC self-renewal and differentiation. Quantitative phosphoproteomics, in vitro kinase assay, site-directed mutagenesis (S563), P body imaging, ESC self-renewal and differentiation assays Cell reports High 39671288
2024 DCP1a and DCP1b are non-redundant cofactors of the mRNA cap hydrolase DCP2 with distinct roles: DCP1a is essential for decapping complex assembly and interactions with mRNA cap-binding proteins, while DCP1b is essential for interactions with protein degradation and translational machinery. DCP1a and DCP1b regulate turnover of distinct sets of mRNAs. Functional dissection by knockdown/knockout, Co-immunoprecipitation of decapping complex components, mRNA turnover profiling Life science alliance Medium 39256052
2021 Dcp1a-deficient mice generated by CRISPR/Cas9 die around embryonic day 10.5 with massive growth retardation and cardiac developmental defects; lethality is fully rescued by transgenic expression of human DCP1A, establishing DCP1A as essential for embryonic growth. CRISPR/Cas9 knockout, transgenic rescue, embryonic phenotyping Biochemical and biophysical research communications High 33813271
2021 Dcp1a puncta are absent in quiescent muscle satellite cells but appear during activation/proliferation. Dcp1a knockdown leads to increased cell proliferation and higher cyclin expression during proliferation but compromised differentiation. Knockdown of Dcp1a leads to increased Fmrp accumulation in puncta, indicating cross-regulation between decay and storage mRNP granules. Single myofiber isolation, live-cell imaging, polysome profiling, siRNA knockdown with proliferation and differentiation assays Skeletal muscle Medium 34238354
2023 Cordycepin suppresses the elevation of DCP1A protein during postovulatory oocyte aging by inhibiting polyadenylation of DCP1A mRNA, consequently impeding maternal mRNA decapping and degradation. Increased DCP1A protein accelerates maternal mRNA degradation during postovulatory aging in both mouse and human oocytes. Proteomic and RNA sequencing analyses, mRNA injection/siRNA in oocytes, polyadenylation assays Cellular and molecular life sciences Medium 38001238
2024 Exogenous Dcp1a mRNA injection into MII oocytes accelerates degradation of maternal mRNAs, while siRNA knockdown of DCP1A reduces maternal mRNA decay in postovulatory-aged oocytes, directly establishing DCP1A as a driver of premature maternal mRNA degradation during postovulatory aging. mRNA microinjection, siRNA knockdown in oocytes, RNA-seq, proteomics Cell proliferation Medium 39629683
2025 SVV 3C protease cleaves DCP1A at Q343, generating fragments that lose the ability to restrict SVV replication. Wild-type DCP1A targets the viral 3D RNA-dependent RNA polymerase for OPTN-mediated autophagic degradation; this antiviral mechanism is abolished after DCP1A cleavage. The cleavage-resistant DCP1A-Q343A mutant retains stronger antiviral effects. Protease cleavage assay, site-directed mutagenesis (Q343A), viral infection assay, autophagy pathway analysis Veterinary research Medium 40022242
2025 DCP1A-containing HOPS condensates under hyperosmotic stress exhibit sub-diffusion due to endoplasmic reticulum attachment and occasional super-diffusion due to coupling to microtubule-dependent active transport, as established by live-cell single-particle tracking. Live-cell single-particle tracking (SPT), ER and microtubule fluorescence labeling, GEM accessibility mapping bioRxivpreprint Low

Source papers

Stage 0 corpus · 29 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies. The Journal of cell biology 75 21859862
2002 SMIF, a Smad4-interacting protein that functions as a co-activator in TGFbeta signalling. Nature cell biology 72 11836524
2013 Maternally recruited DCP1A and DCP2 contribute to messenger RNA degradation during oocyte maturation and genome activation in mouse. Biology of reproduction 66 23136299
2013 The P body protein Dcp1a is hyper-phosphorylated during mitosis. PloS one 54 23300942
2018 MALAT1 promotes the colorectal cancer malignancy by increasing DCP1A expression and miR203 downregulation. Molecular carcinogenesis 38 29964337
2020 Porcine Deltacoronavirus nsp5 Cleaves DCP1A To Decrease Its Antiviral Activity. Journal of virology 35 32461317
2018 Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 4 Cleaves Porcine DCP1a To Attenuate Its Antiviral Activity. Journal of immunology (Baltimore, Md. : 1950) 31 30158128
2013 mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain. The Journal of biological chemistry 27 24382890
2023 The main protease of SARS-CoV-2 cleaves histone deacetylases and DCP1A, attenuating the immune defense of the interferon-stimulated genes. The Journal of biological chemistry 26 36758802
2013 Phosphorylation of mRNA decapping protein Dcp1a by the ERK signaling pathway during early differentiation of 3T3-L1 preadipocytes. PloS one 23 23637887
2019 Bta-miR-34b regulates milk fat biosynthesis by targeting mRNA decapping enzyme 1A (DCP1A) in cultured bovine mammary epithelial cells1. Journal of animal science 21 31278739
2019 LINC00339 promotes gastric cancer progression by elevating DCP1A expression via inhibiting miR-377-3p. Journal of cellular physiology 19 31188482
2016 Genetic variants in the PIWI-piRNA pathway gene DCP1A predict melanoma disease-specific survival. International journal of cancer 18 27578485
2012 Lafora disease E3 ubiquitin ligase malin is recruited to the processing bodies and regulates the microRNA-mediated gene silencing process via the decapping enzyme Dcp1a. RNA biology 17 23131811
2008 Dcp1a phosphorylation along neuronal development and stress. FEBS letters 17 19084008
2020 Circ_0007031 Serves as a Sponge of miR-760 to Regulate the Growth and Chemoradiotherapy Resistance of Colorectal Cancer via Regulating DCP1A. Cancer management and research 16 32982440
2023 Cordycepin delays postovulatory aging of oocytes through inhibition of maternal mRNAs degradation via DCP1A polyadenylation suppression. Cellular and molecular life sciences : CMLS 13 38001238
2017 Dcp1a and GW182 Induce Distinct Cellular Aggregates and Have Different Effects on microRNA Pathway. DNA and cell biology 10 28488892
2023 Swine acute diarrhoea syndrome coronavirus (SADS-CoV) Nsp5 antagonizes type I interferon signaling by cleaving DCP1A. Frontiers in immunology 9 37283741
2021 mRNP granule proteins Fmrp and Dcp1a differentially regulate mRNP complexes to contribute to control of muscle stem cell quiescence and activation. Skeletal muscle 9 34238354
2020 Expression of DCP1a in gastric cancer and its biological function and mechanism in chemotherapy resistance in gastric cancer cells. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 7 32646734
2025 The Seneca Valley virus 3C protease cleaves DCP1A to attenuate its antiviral effects. Veterinary research 6 40022242
2023 LncRNA HOXD-AS2 regulates miR-3681-5p/DCP1A axis to promote the progression of non-small cell lung cancer. Journal of thoracic disease 6 37065560
2021 mRNA decapping factor Dcp1a is essential for embryonic growth in mice. Biochemical and biophysical research communications 6 33813271
2024 Multi-omics revealed that DCP1A and SPDL1 determine embryogenesis defects in postovulatory ageing oocytes. Cell proliferation 3 39629683
2024 Non-redundant roles for the human mRNA decapping cofactor paralogs DCP1a and DCP1b. Life science alliance 2 39256052
2024 DCP1A, a MEK substrate, regulates the self-renewal and differentiation of mouse embryonic stem cells. Cell reports 2 39671288
2024 Erratum to lncRNA HOXD-AS2 regulates miR-3681-5p/DCP1A axis to promote the progression of non-small cell lung cancer. Journal of thoracic disease 0 38410577
2024 RETRACTION: LINC00339 promotes gastric cancer progression by elevating DCP1A expression via inhibiting miR-377-3p. Journal of cellular physiology 0 39348227

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