| 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 |
|