Affinage

SNRPD3

Small nuclear ribonucleoprotein Sm D3 · UniProt P62318

Round 2 corrected
Length
126 aa
Mass
13.9 kDa
Annotated
2026-04-28
46 papers in source corpus 17 papers cited in narrative 17 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SNRPD3 (SmD3) is a core Sm ring protein that assembles with six other Sm subunits into a heteroheptameric ring on spliceosomal snRNAs, functioning as an essential component of the spliceosome required for pre-mRNA splicing, snRNP biogenesis, and cell viability (PMID:10025403, PMID:12226669, PMID:34703654). Its arginine-glycine-rich C-terminal tail is symmetrically dimethylated by the PRMT5–pICln methylosome complex, after which SmD3 is transferred to the SMN complex for snRNP core assembly; within U1 snRNP, SmD3 residues Glu37/Asp38 directly contact U1C to stabilize the U1–5′ splice site duplex (PMID:11713266, PMID:24497193). Beyond canonical splicing, SmD3 haploinsufficiency selectively reduces U4/U5 snRNA levels and intronic snoRNA biogenesis, and MYCN recruits SmD3 and PRMT5 into a trimeric complex that maintains balanced alternative splicing of cell-cycle regulators in neuroblastoma (PMID:22869524, PMID:38049564, PMID:38049564). A recurrent cancer-associated G96V mutation in the Sm ring domain alters splicing under hypoxia—including mis-splicing of DNM1L—linking SmD3 integrity to mitochondrial dynamics and stress adaptation (PMID:38241813).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1997 High

    Establishing that SmD3 is a direct binding partner of SMN placed Sm proteins in a biogenesis pathway relevant to spinal muscular atrophy and identified the SMN complex as the assembly machine for snRNP cores.

    Evidence Co-immunoprecipitation and direct pull-down assays between SMN/SIP1 and individual Sm proteins

    PMID:9323129

    Open questions at the time
    • Mechanism by which SMN facilitates Sm ring closure was not resolved
    • Whether all seven Sm proteins require SMN for assembly was unclear
  2. 1999 High

    Solving the crystal structures of Sm heterodimers (D3–B and D1–D2) established the common Sm fold and provided the first structural evidence that seven Sm proteins form a closed ring through which snRNA threads.

    Evidence X-ray crystallography of recombinant Sm protein complexes

    PMID:10025403

    Open questions at the time
    • Full heptameric ring structure on RNA was not yet determined
    • SmD3-specific contacts to snRNA were not resolved at atomic level
  3. 2001 High

    Discovery of the PRMT5–pICln methylosome as the enzyme that symmetrically dimethylates SmD3 C-terminal arginines, and identification of a 6S pICln–SmD1–SmD3 intermediate, defined the biochemical pathway upstream of SMN-dependent snRNP assembly.

    Evidence Biochemical fractionation, in vitro methyltransferase assays, co-immunoprecipitation, and mass spectrometry from two independent labs

    PMID:11713266 PMID:11747828

    Open questions at the time
    • Whether sDMA is strictly required for SMN binding or merely facilitatory was debated
    • Structural basis of pICln's inhibition of premature Sm ring closure was unknown
  4. 2002 High

    Proteomic identification of SmD3 in purified functional spliceosomes confirmed it as a bona fide spliceosome component, while Drosophila loss-of-function studies demonstrated that SmD3 is essential for organismal viability and tissue growth control.

    Evidence LC-MS/MS of affinity-purified human spliceosomes; P-element mutagenesis with transgenic rescue in Drosophila

    PMID:12072471 PMID:12226669

    Open questions at the time
    • Which specific splicing events are most sensitive to SmD3 reduction was undefined
    • Whether overgrowth phenotype in Drosophila reflects splicing-independent roles was untested
  5. 2004 High

    In vivo metabolic labeling confirmed sDMA on SmD3 as a major autoantibody epitope in SLE, yet mutagenesis showed sDMA is dispensable for snRNP assembly and nuclear import, separating the modification's immunological significance from its role in core snRNP biogenesis.

    Evidence Heavy methyl SILAC LC-MS/MS for in vivo sDMA; site-directed mutagenesis of SmD3 RG-domain arginines with cellular assembly and localization assays

    PMID:15642139 PMID:15782174 PMID:16236255

    Open questions at the time
    • Whether sDMA affects SmD3 function in vivo beyond assembly (e.g., splicing fidelity or chromatin interactions) was not tested
    • Dispensability conclusion based on overexpression system—endogenous replacement not performed
  6. 2012 Medium

    SmD3 haploinsufficiency selectively reduced U4 and U5 snRNA levels and downstream intronic snoRNA biogenesis without globally disrupting pre-mRNA splicing, revealing a non-splicing function of SmD3 in noncoding RNA metabolism.

    Evidence Retroviral promoter-trap mutagenesis in CHO cells; RT-qPCR and northern blotting for snRNAs and snoRNAs

    PMID:22869524

    Open questions at the time
    • Mechanism by which SmD3 dosage specifically affects U4/U5 but not other snRNAs is unclear
    • Whether snoRNA loss drives the metabolic stress phenotype was not causally tested
    • Single cell line system (CHO)
  7. 2014 High

    Structure-guided mutagenesis of SmD3 Glu37/Asp38 in yeast showed these residues directly stabilize the U1 snRNP–5′ splice site interaction via contacts with U1C, placing SmD3 at the heart of early splice-site recognition.

    Evidence Yeast genetics: structure-guided alanine mutagenesis, synthetic lethality with mud2Δ, bypass of Prp28 essentiality

    PMID:24497193

    Open questions at the time
    • Whether equivalent contacts are functionally important in human U1 snRNP was not directly tested
    • Quantitative contribution of SmD3–U1C contact versus other stabilizing interactions was not measured
  8. 2015 High

    Systematic mutagenesis of SmD3's RNA-binding triad revealed built-in redundancy within the Sm ring: no single SmD3 RNA-contact residue is essential, but combined loss with SmB residues is lethal, and SmD3 mutations show genetic interactions with U2 snRNP components.

    Evidence Alanine-scanning mutagenesis and double-mutant synthetic lethality screens in yeast

    PMID:25897024

    Open questions at the time
    • Whether redundancy exists in metazoan Sm rings was not tested
    • Which specific pre-mRNA substrates are most affected by SmD3 RNA-binding mutations is unknown
  9. 2021 Medium

    CRISPRi and shRNA depletion of SNRPD3 in human cancer cells caused p53-dependent senescence or mitotic catastrophe, and overexpression rescued viability, establishing SNRPD3 as essential for human cell proliferation and survival.

    Evidence CRISPRi knockdown, inducible shRNA, overexpression rescue, flow cytometry in A549 and U251 cells

    PMID:34703654

    Open questions at the time
    • Whether lethality is due to global splicing failure or specific transcript mis-splicing was not resolved
    • Non-cancer cell types were not examined
  10. 2023 High

    MYCN was shown to directly bind SmD3 and recruit PRMT5 into a trimeric complex, transcriptionally upregulating SNRPD3 and maintaining balanced alternative splicing of cell-cycle genes (BIRC5, CDK10) critical for neuroblastoma growth—linking an oncogenic transcription factor to spliceosome function via SmD3.

    Evidence Reciprocal co-IP of MYCN–SNRPD3–PRMT5 complex, RNA-seq for alternative splicing, shRNA knockdown, in vivo tumorigenicity, PRMT5 inhibitor treatment in neuroblastoma cells

    PMID:38049564

    Open questions at the time
    • Whether the MYCN–SmD3–PRMT5 complex operates in non-neuroblastoma MYCN-amplified cancers is untested
    • Direct RNA targets of the trimeric complex beyond BIRC5/CDK10 are uncharacterized
  11. 2024 Medium

    A recurrent pan-cancer SmD3 G96V mutation was found to confer hypoxia resistance by mis-splicing DNM1L (DRP1), causing excessive mitochondrial fragmentation reversible by DRP1 inhibition—demonstrating that Sm ring integrity controls stress-adaptive splicing with mitochondrial consequences.

    Evidence Isogenic cell line engineering with G96V, RNA-seq under hypoxia, mitochondrial morphology imaging, Mdivi-1 treatment

    PMID:38241813

    Open questions at the time
    • Whether G96V alters Sm ring stability or snRNA binding was not structurally determined
    • Generalizability across cancer types in vivo is unconfirmed
    • Single isogenic model system

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis of the MYCN–SmD3–PRMT5 trimeric complex, whether SmD3 sDMA modification modulates splicing fidelity or chromatin interactions in vivo (as suggested by preprint data on PRMT5 inhibition causing SmD3 chromatin detention), and how SmD3 dosage selectively controls specific snRNA and snoRNA levels.
  • No structural model of MYCN–SmD3–PRMT5 complex exists
  • In vivo endogenous replacement of SmD3 sDMA-site mutants has not been performed in mammalian cells
  • Mechanism of selective snRNA sensitivity to SmD3 dosage is undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0005198 structural molecule activity 3
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 2
Pathway
R-HSA-8953854 Metabolism of RNA 7 R-HSA-1643685 Disease 3 R-HSA-392499 Metabolism of proteins 3 R-HSA-1640170 Cell Cycle 2
Partners
CLNS1AMYCNPRMT5SMN1SNRPBSNRPCSNRPD1
Complex memberships
MYCN-SNRPD3-PRMT5 complexPRMT5-pICln methylosome (6S intermediate with SmD1-SmD3-pICln)Sm core heptamer (SmB/B'-SmD1-SmD2-SmD3-SmE-SmF-SmG)

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 Crystal structures of the Sm protein heterodimers D3B and D1D2 revealed that Sm proteins share a common fold: an N-terminal alpha-helix followed by a strongly bent five-stranded antiparallel beta-sheet. The D3B and D1D2 dimers superpose closely in their core regions, and the structures suggest that the seven Sm proteins (including SmD3) form a closed ring through which snRNA is threaded via the positively charged central hole. X-ray crystallography of recombinant Sm protein complexes Cell High 10025403
1997 SMN (Survival of Motor Neurons), the spinal muscular atrophy disease gene product, directly interacts with multiple spliceosomal snRNP Sm core proteins including SmD3 (D1, D2, D3, B, and E). This interaction places SMN in a complex with snRNP Sm proteins and implicates SMN in snRNP biogenesis. Co-immunoprecipitation and direct binding assays (pull-down) between SMN/SIP1 and individual Sm proteins Cell High 9323129
2001 The methylosome, a 20S complex containing the methyltransferase JBP1 (PRMT5) and pICln, symmetrically dimethylates arginine (sDMA) residues in the RG-rich C-terminal domains of SmD3 (and SmD1). Unmodified SmD3 associates with the methylosome via its RG domain, and after sDMA modification, SmD3 is transferred to the SMN complex for snRNP core particle assembly. A 6S intermediate complex containing pICln, SmD1, and SmD3 (but not JBP1) was also identified. Biochemical fractionation, co-immunoprecipitation, in vitro methyltransferase assay, mass spectrometry Molecular and cellular biology High 11713266
2001 A complex containing PRMT5, pICln, and Sm proteins (including SmD3) catalyzes symmetrical dimethylarginine (sDMA) modification of SmD3 and SmD1. pICln binds the Sm fold of Sm proteins and inhibits spontaneous Sm core assembly onto U snRNA by preventing Sm-Sm interactions needed for ring formation, suggesting the pICln-PRMT5 complex regulates an early step in snRNP biogenesis. Co-immunoprecipitation, in vitro methyltransferase assay, Sm core assembly assay Current biology : CB High 11747828
2002 Comprehensive mass spectrometry-based proteomic analysis of purified functional human spliceosomes identified SmD3 (SNRPD3) as a confirmed component of the spliceosomal machinery, establishing its presence in the intact spliceosome complex. Affinity purification of functional spliceosomes followed by nanoscale LC-MS/MS Nature High 12226669
2002 Drosophila Sm D3 is encoded in the reverse orientation within the first intron of the Ornithine Decarboxylase Antizyme gene. P-element insertions in the 5'-UTR or promoter of SmD3 specifically reduce or abolish SmD3 expression, causing embryonic lethality (amorphic alleles) or larval lethality with overgrown imaginal discs, brain hemispheres, and hematopoietic organs (hypomorphic alleles). These phenotypes are rescued by an SmD3+ transgene, demonstrating that SmD3 loss specifically underlies the gutfeeling phenotype. P-element insertion mutagenesis, transgenic rescue, immunostaining, genetic complementation Genetics High 12072471
2004 The symmetrical dimethylarginine (sDMA) post-translational modification on SmD3 is not required for snRNP assembly or nuclear transport. Mutating the modified arginine residues to leucines in SmD3 did not prevent its assembly into snRNPs or its nuclear import in transiently expressed SmD3 variants. Site-directed mutagenesis of SmD3 arginine residues, transfection, subcellular fractionation, and immunoprecipitation Biochemical and biophysical research communications Medium 16236255
2004 SmD3 and SmD1 contain symmetrical dimethylarginine (sDMA) residues in their C-termini. Heavy methyl SILAC mass spectrometry confirmed sDMA as an in vivo modification on these Sm proteins, and the dimethylated arginine represents a major antigenic determinant of anti-Sm autoantibodies in SLE. A synthetic sDMA-containing SmD3 peptide (amino acids 108-122) was shown to be immunoreactive with a specific subset of anti-Sm antibodies. Heavy methyl SILAC (stable isotope labeling) combined with LC-MS/MS; ELISA with dimethylated and unmodified peptides Arthritis research & therapy / Nature methods High 15642139 15782174
2012 Haploinsufficiency of SmD3 (SNRPD3) in Chinese hamster ovary cells reduces the levels of snRNAs U4 and U5, which in turn decreases snoRNA-containing intron lariat abundance and snoRNA expression, even though pre-mRNA splicing per se is maintained. This identifies SmD3 as a critical upstream regulator of intronic noncoding RNA (snoRNA) biogenesis and metabolic stress response pathways. Retroviral promoter trap mutagenesis to generate SmD3 haploinsufficient cells; RT-qPCR and northern blotting for snRNAs, snoRNAs, and intron lariats; splicing assays Molecular and cellular biology Medium 22869524
2014 In yeast U1 snRNP, SmD3 residues Glu37 and Asp38 make direct contacts with Arg21 of the U1C subunit (Yhc1), fortifying the U1•5' splice site (5'SS) duplex complex. Mutations at these SmD3 residues synergize genetically with mud2Δ and bypass the essentiality of DEAD-box ATPase Prp28, consistent with destabilization of U1•5'SS interaction. Genetic interaction analysis also showed SmD3's role in pre-mRNA 5' splice site recognition within U1 snRNP. Mutational analysis guided by human U1 snRNP structure; synthetic lethality/sickness screens; prp28Δ bypass assay in yeast Nucleic acids research High 24497193
2015 Mutagenesis of the RNA-binding triad of SmD3 (Ser-Asn-Arg) revealed built-in redundancy in the Sm ring: no single residue of the RNA-binding triad is individually essential, but simultaneous mutations of Asn or Arg in both SmD3 and SmB are lethal. SmD3 RNA-binding mutations are synthetically lethal with loss of U2 snRNP subunit Lea1, placing SmD3's RNA contacts in a functional relationship with U2 snRNP. C-terminal truncations of SmD3 are lethal without Mud2 or Lea1 and viable without Nam8/Mud1. SMD3-E35A specifically suppresses temperature sensitivity of lea1Δ. Yeast genetics: alanine-scanning mutagenesis, synthetic lethality analysis, double-mutant growth assays RNA (New York, N.Y.) High 25897024
2019 In Drosophila, SmD3 is required for germline stem cell (GSC) niche maintenance and controls self-renewal and differentiation of GSCs in the testis. SmD3 physically interacts with ribosomal protein RpL18 (a large ribosomal subunit regulator) as identified by LC-MS/MS, and regulates both spliceosome and ribosome subunit expression levels via RpL18, revealing crosstalk between the spliceosome and ribosome. Genetic manipulation in Drosophila (loss-of-function), in vitro proliferation/apoptosis assays in S2 cells, LC-MS/MS interactome, western blotting FASEB journal Medium 30921522
2021 CRISPRi knockdown of SNRPD3 in human A549 and U251 cells induces apoptosis (murine cells) or senescence/mitotic catastrophe depending on p53 status (human tumor cells), confirming that SNRPD3 is essential for cell viability. Overexpression of SNRPD3 rescues U251 cells from mitotic catastrophe induced by shRNA targeting SNRPD3, directly linking SNRPD3 expression level to cell survival outcome. CRISPRi knockdown, inducible shRNA expression, overexpression rescue, flow cytometry, cell viability assays Molecular therapy. Nucleic acids Medium 34703654
2023 MYCN directly binds SNRPD3 protein and recruits PRMT5 into a trimeric complex, leading to increased symmetrical dimethylarginine methylation of SNRPD3. MYCN transcriptionally upregulates SNRPD3 expression, and the MYCN-SNRPD3 complex maintains balanced alternative splicing of cell cycle regulators (including BIRC5 and CDK10) required for neuroblastoma cell growth. Depletion of SNRPD3 in the presence of MYCN overexpression causes excessive differential splicing. PRMT5 inhibition (JNJ-64619178) reduces SNRPD3 methylation and cell viability in neuroblastoma cells with high SNRPD3/MYCN expression. Co-immunoprecipitation (MYCN-SNRPD3-PRMT5 complex), RNA-sequencing (alternative splicing analysis), shRNA knockdown, colony formation, in vivo tumorigenicity, PRMT5 inhibitor treatment Oncogene High 38049564
2024 A cancer-associated point mutation in SNRPD3 (G96V, a pan-cancer hotspot in the Sm ring) confers resistance to hypoxia. RNA-seq of G96V mutant cells under hypoxia revealed numerous differentially spliced events, including skipping of exons in DNM1L mRNA (encoding DRP1). G96V mutant cells exhibited excessive mitochondrial fragmentation due to altered DRP1-mediated fission, and treatment with DRP1 inhibitor Mdivi-1 reversed hypoxia resistance in G96V mutant cells. Cancer mutation analysis, isogenic cell line engineering, RNA-seq, mitochondrial morphology imaging, DRP1 inhibitor (Mdivi-1) treatment, cell viability assays under hypoxia Biochemical and biophysical research communications Medium 38241813
2026 SNRPD3 promotes endometrial cancer cell proliferation, migration, and invasion by regulating splicing of SREBF1 mRNA; silencing SNRPD3 causes intron retention in SREBF1. Depletion of SREBF1 abolishes the enhanced proliferative and lipid metabolic capacity of SNRPD3-overexpressing cells, placing SNRPD3 upstream of SREBF1 in a splicing-dependent oncogenic pathway. Antisense oligonucleotide (ASO)-mediated silencing of SNRPD3 suppresses tumor growth in patient-derived xenograft models. shRNA/siRNA knockdown, overexpression, RNA-seq (intron retention analysis), subcutaneous xenograft, PDX model, ASO treatment Biochemical and biophysical research communications Medium 41924775
2024 PRMT5 inhibition and knockdown of the PRMT5 adapter pICln (CLNS1A) causes detention of SNRPD3 protein on chromatin along with genomically retained, incompletely processed polyadenylated transcripts (GRIPPs). Arginine methylation of snRNPs (including SNRPD3) by PRMT5 is critical for their homeostatic chromatin and RNA interactions, and is required for mRNA chromatin escape and subsequent nuclear export. PRMT5 inhibition and pICln knockdown; spike-in controlled fractionated transcriptomics; fractionated cell proteomics; inducible isogenic wildtype and arginine-mutant SNRPB (with implications for SNRPD3 co-fractionation) bioRxivpreprint Medium

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2012 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Molecular cell 973 22681889
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2008 Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell 787 18854154
2002 Directed proteomic analysis of the human nucleolus. Current biology : CB 780 11790298
2002 Comprehensive proteomic analysis of the human spliceosome. Nature 725 12226669
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
1997 The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell 569 9323129
2017 Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15. Science (New York, N.Y.) 533 28302793
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2010 Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science (New York, N.Y.) 421 20360068
2013 The intracellular interactome of tetraspanin-enriched microdomains reveals their function as sorting machineries toward exosomes. The Journal of biological chemistry 413 23463506
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2011 IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA. Nature immunology 405 21642987
1999 Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 374 10025403
2015 Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry. Nature methods 370 26414014
2007 Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Molecular cell 367 17643375
2004 Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nature methods 364 15782174
2001 The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. Molecular and cellular biology 354 11713266
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2003 Splicing double: insights from the second spliceosome. Nature reviews. Molecular cell biology 329 14685174
2001 Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Current biology : CB 323 11747828
2010 Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 318 21145461
2007 Location of a possible miRNA processing site in SmD3/SmB nuclear bodies in Arabidopsis. Plant & cell physiology 111 17675322
2004 Identification of a SmD3 epitope with a single symmetrical dimethylation of an arginine residue as a specific target of a subpopulation of anti-Sm antibodies. Arthritis research & therapy 59 15642139
1998 The Drosophila gene for antizyme requires ribosomal frameshifting for expression and contains an intronic gene for snRNP Sm D3 on the opposite strand. Molecular and cellular biology 34 9488472
2011 Knock-out mutations of Arabidopsis SmD3-b induce pleotropic phenotypes through altered transcript splicing. Plant science : an international journal of experimental plant biology 29 21421416
2005 Improved serological differentiation between systemic lupus erythematosus and mixed connective tissue disease by use of an SmD3 peptide-based immunoassay. Clinical and diagnostic laboratory immunology 22 15642993
2014 Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28. Nucleic acids research 20 24497193
2019 Small ribonucleoprotein particle protein SmD3 governs the homeostasis of germline stem cells and the crosstalk between the spliceosome and ribosome signals in Drosophila. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 18 30921522
2012 SmD3 regulates intronic noncoding RNA biogenesis. Molecular and cellular biology 18 22869524
2015 Structure-function analysis and genetic interactions of the Yhc1, SmD3, SmB, and Snp1 subunits of yeast U1 snRNP and genetic interactions of SmD3 with U2 snRNP subunit Lea1. RNA (New York, N.Y.) 17 25897024
2021 Arabidopsi s Spliceosome Factor SmD3 Modulates Immunity to Pseudomonas syringae Infection. Frontiers in plant science 14 34925413
2002 P elements inserted in the vicinity of or within the Drosophila snRNP SmD3 gene nested in the first intron of the Ornithine Decarboxylase Antizyme gene affect only the expression of SmD3. Genetics 9 12072471
2023 MYCN and SNRPD3 cooperate to maintain a balance of alternative splicing events that drives neuroblastoma progression. Oncogene 8 38049564
2021 Non-targeting control for MISSION shRNA library silences SNRPD3 leading to cell death or permanent growth arrest. Molecular therapy. Nucleic acids 8 34703654
2005 The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport. Biochemical and biophysical research communications 6 16236255
2024 Cancer-associated SNRPD3 mutation confers resistance to hypoxia, which is attenuated by DRP1 inhibition. Biochemical and biophysical research communications 2 38241813
2026 SNRPD3 promotes endometrial cancer progression via regulating SREBF1 intron retention. Biochemical and biophysical research communications 0 41924775