Affinage

GEMIN5

Gem-associated protein 5 · UniProt Q8TEQ6

Length
1508 aa
Mass
168.6 kDa
Annotated
2026-04-28
52 papers in source corpus 32 papers cited in narrative 32 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

GEMIN5 is a multidomain RNA-binding protein that serves dual roles as the snRNA-recognition subunit of the SMN complex and as a ribosome-associated translational regulator. Its N-terminal tandem WD40 domains specifically recognize the Sm site and m7G cap of spliceosomal pre-snRNAs, delivering them to the SMN complex for Sm core assembly during snRNP biogenesis; this recognition is selective for spliceosomal snRNAs and excludes U7 snRNA (PMID:16857593, PMID:27881600, PMID:40592581). A central TPR-like dimerization domain mediates self-assembly, interaction with SMN, Gemin2, and Gemin4, and is regulated by phosphorylation to control ribosome association and translational output, while the C-terminal non-canonical RNA-binding domain assembles into a homodecameric architecture that binds IRES elements and select mRNAs to repress global translation yet selectively enhance translation of ribosomal protein and histone mRNAs (PMID:31799608, PMID:36056043, PMID:35987821, PMID:36420152). Biallelic loss-of-function variants in GEMIN5 cause a neurodevelopmental syndrome (NEDCAM) with cerebellar atrophy, motor dysfunction, and disrupted snRNP assembly, which can be partially rescued by SMN upregulation (PMID:33963192, PMID:37369805).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2001 High

    Identification of GEMIN5 as a WD-repeat subunit of the SMN complex established it as a new player in the snRNP biogenesis machinery, answering how the SMN complex achieves substrate recognition breadth through additional components beyond the SMN-Gemin2 core.

    Evidence Co-immunoprecipitation, direct binding to SMN, and co-localization with SMN in gems in HeLa cells

    PMID:11714716

    Open questions at the time
    • The RNA-binding activity of Gemin5 was not yet demonstrated
    • No structural information on the WD40 domains
    • Mechanism of snRNA recognition unknown
  2. 2006 High

    Demonstrating that Gemin5 is the snRNA-binding factor of the SMN complex resolved a longstanding question of how pre-snRNAs are captured for Sm core assembly, establishing Gemin5 as the specificity determinant that reads the Sm site.

    Evidence Direct RNA-binding assays and RNAi knockdown reducing snRNP assembly in human cells

    PMID:16857593

    Open questions at the time
    • Which domain mediates snRNA binding was unknown
    • Structural basis of Sm site recognition unresolved
    • Connection to translation machinery not yet explored
  3. 2008 High

    Discovery that Gemin5 represses both cap-dependent and IRES-driven translation and binds viral IRES elements revealed an unexpected second function beyond snRNP biogenesis, linking it to translational control.

    Evidence Riboproteomics, UV-crosslinking immunoprecipitation, shRNA depletion with in vitro translation assays

    PMID:19066202

    Open questions at the time
    • Which region of Gemin5 mediates IRES binding was unknown
    • Mechanism of translation repression uncharacterized
    • Relationship between snRNA-binding and translation functions unclear
  4. 2009 High

    Mapping snRNA binding and m7G cap recognition to the N-terminal WD40 domain, with identification of specific contact residues, established the molecular basis by which Gemin5 reads the dual signals (Sm site and cap) on pre-snRNAs.

    Evidence Deletion analysis, hydroxyl radical probing, mass spectrometry mapping, cap-affinity chromatography, UV crosslinking, and site-directed mutagenesis

    PMID:19377484 PMID:19750007

    Open questions at the time
    • No atomic-resolution structure yet
    • How Gemin5 hands off snRNA to the SMN complex for Sm ring assembly was unclear
  5. 2010 High

    Isolation of a transient pre-snRNA–Gemin5 intermediate and demonstration that Gemin5 delivers pre-snRNAs as substrates to the SMN complex clarified the kinetic pathway of snRNP biogenesis, placing Gemin5 as the upstream capture agent.

    Evidence Formaldehyde crosslinking riboproteomics with high-throughput sequencing in human cells treated with protein synthesis inhibitors

    PMID:20513430

    Open questions at the time
    • Mechanism of substrate handoff from Gemin5 to the Sm ring assembly machinery not resolved
    • Fate of Gemin5 after delivery unknown
  6. 2012 High

    Assigning IRES-binding and translation-repression activity to the C-terminal region (distinct from the N-terminal snRNA-binding WD40 domain) established GEMIN5 as a modular protein with separable RNA-recognition and translation-regulatory functions.

    Evidence Purified protein binding assays, SHAPE structural analysis, and translation assays with domain truncations

    PMID:22362733 PMID:23221641

    Open questions at the time
    • Atomic structure of C-terminal RNA-binding domain lacking
    • Selectivity of mRNA targets beyond IRES elements unknown
  7. 2014 High

    Identification of two non-canonical bipartite RNA-binding sites (RBS1 and RBS2) in the C-terminal domain, with RBS2 as the minimal translation-repression module, defined the architecture of GEMIN5's translational regulatory region at residue-level resolution.

    Evidence Purified protein RNA-binding assays, NMR structure in solution, translation reporter assays

    PMID:24598255

    Open questions at the time
    • How RBS1 and RBS2 cooperate within the full-length protein was unclear
    • Structural basis of the homodecamer not yet known
  8. 2016 High

    Crystal structures of the tandem WD40 domains in complex with the Sm site and m7G cap provided atomic-level understanding of how GEMIN5 achieves sequence-specific snRNA recognition, while ribosome-binding studies via the same N-terminal domain revealed a direct role in translation elongation control through contacts with ribosomal proteins L3 and L4.

    Evidence X-ray crystallography with ITC and mutagenesis; subcellular fractionation, pull-down of ribosomes, polysome profiling

    PMID:27507887 PMID:27881600 PMID:27881601

    Open questions at the time
    • How the same WD40 domain coordinates snRNA binding and ribosome association was not resolved
    • In vivo relevance of ribosome binding for specific mRNA translation unknown
  9. 2018 High

    Discovery that Gemin5's RBS1 domain preferentially binds its own mRNA stem-loop to autoregulate translation established a cis-regulatory feedback mechanism, and Gemin5's role in disposing of unassembled U1 snRNA via P-body targeting was defined.

    Evidence CLIP, RNA immunoprecipitation, translation reporter assays with stem-loop mutagenesis; Co-IP and immunofluorescence in SMN-deficient cells with Gemin5 knockdown

    PMID:29537490 PMID:29771365

    Open questions at the time
    • Whether autoregulation operates in disease-relevant tissues was untested
    • Mechanism of P-body targeting unclear
  10. 2020 High

    Crystal structure of the central TPR-like dimerization domain revealed it as a canoe-shaped dimer serving as the protein–protein interaction hub; disruption of dimerization abolished the translation-enhancing activity of the viral cleavage fragment p85, connecting oligomerization to functional output.

    Evidence Crystal structure determination, mutagenesis disrupting dimerization, Co-IP in living cells, translation assays

    PMID:31799608

    Open questions at the time
    • How dimerization integrates with decamerization of the C-terminal domain was unknown
    • Physiological signals regulating dimerization not identified
  11. 2021 High

    Patient-derived neurons with biallelic GEMIN5 mutations showed disrupted snRNP assembly, altered GEMIN5 stability and interactome, and Drosophila knockdown recapitulated motor dysfunction, establishing GEMIN5 as the causative gene for NEDCAM neurodevelopmental syndrome.

    Evidence iPSC-derived neuron studies, snRNP assembly assays, Drosophila knockdown with behavioral phenotyping

    PMID:33963192

    Open questions at the time
    • Relative contributions of snRNP biogenesis defects vs. translation dysregulation to neurodegeneration unclear
    • No therapeutic intervention tested at this point
  12. 2022 High

    The C-terminal domain was shown to adopt a homodecameric (dimer of pentamers) architecture required for RNA binding and translation regulation, while disease variants in the TPR domain disrupted dimerization and ribosome association, and phosphorylation at T897 modulated the translational interactome — collectively revealing how oligomeric state and post-translational modification control GEMIN5 output.

    Evidence Cryo-EM/crystal structures, mutagenesis, ribosome binding assays, MS-based interactome of disease variants, polysome profiling with TOP motif mutagenesis

    PMID:35393353 PMID:35987821 PMID:36056043 PMID:36420152

    Open questions at the time
    • Kinase(s) responsible for T897 phosphorylation not identified
    • How decamerization and TPR dimerization are coordinated in full-length protein unknown
    • Structural basis for selective mRNA recognition (TOP/histone) not resolved
  13. 2023 Medium

    Mapping the SMN–Gemin5 interaction to SMN's Tudor domain and the Gemin5 C-terminus, and demonstrating that SMN upregulation rescues GEMIN5-loss phenotypes in neurons and flies, identified a potential therapeutic axis for NEDCAM through existing SMA therapeutics.

    Evidence Co-IP domain mapping, SMN Tudor domain mutagenesis, gene therapy and ASO rescue in iPSC neurons and Drosophila, snRNP assembly assays

    PMID:37369805

    Open questions at the time
    • Rescue was partial; long-term efficacy and safety in mammalian models not assessed
    • Whether SMN rescue addresses translation-regulatory deficits of GEMIN5 mutants is untested
  14. 2025 Medium

    Phosphorylation at Ser/Thr 847–854 in the dimerization domain was shown to regulate ribosome binding and cap-dependent translation, and dsRNA-mimic stress enhanced Gemin5–RNA interaction, connecting stress signaling to Gemin5 translational regulation; separately, Gemin5 was shown to exclude U7 snRNA, defining the boundary of its substrate specificity.

    Evidence Mutagenesis with ribosome binding and translation assays; affinity pulldown with U7 snRNA followed by mass spectrometry

    PMID:40592581 PMID:40734649

    Open questions at the time
    • In vivo phosphorylation dynamics under stress not characterized
    • Whether U7 exclusion is solely determined by Sm site sequence divergence or involves additional factors is unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include how GEMIN5's snRNP biogenesis and translational regulatory functions are coordinated in full-length protein in vivo, which kinases phosphorylate the TPR domain, and whether the translation-regulatory defects contribute independently to NEDCAM pathogenesis beyond snRNP assembly impairment.
  • No full-length GEMIN5 structure integrating WD40, TPR, and C-terminal decamer domains
  • Kinase identity for TPR phosphoresidues unknown
  • Relative pathogenic contribution of translation vs. splicing dysfunction in NEDCAM undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 8 GO:0005198 structural molecule activity 3 GO:0045182 translation regulator activity 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005840 ribosome 4 GO:0005829 cytosol 3 GO:0005634 nucleus 1
Pathway
R-HSA-8953854 Metabolism of RNA 8 R-HSA-392499 Metabolism of proteins 4 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-5357801 Programmed Cell Death 1
Partners
GEMIN2GEMIN4HSPA8MAP2K4MAP3K5RPL3RPL4SMN
Complex memberships
SMN complex

Evidence

Reading pass · 32 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Gemin5 is a novel WD repeat protein component of the SMN complex that binds SMN directly and interacts with snRNP core proteins SmB, SmD1, SmD2, SmD3, and SmE. It colocalizes with SMN in cytoplasmic and nuclear gems. Co-immunoprecipitation, direct binding assays, immunolocalization The Journal of biological chemistry High 11714716
2006 Gemin5 is the snRNA-binding protein of the SMN complex, binding directly and specifically to the Sm site and unique features of snRNAs. Reduction of Gemin5 reduces SMN complex capacity to bind snRNAs and assemble Sm cores. Direct RNA-binding assays, RNAi knockdown with snRNP assembly readout Molecular cell High 16857593
2006 Gemin5 interacts directly with eIF4E through a YXXXXLPhi motif and co-localizes with eIF4E in cytoplasmic P-bodies. Quantitative proteomics (cap-affinity chromatography), Co-IP, immunofluorescence co-localization Journal of proteome research Medium 16739988
2007 Gemin5 is predominantly cytoplasmic and largely absent from nuclear SMN complexes in gems/Cajal bodies, suggesting its role is restricted to cytoplasmic snRNA capture for SMN complex delivery to the nucleus. Subcellular fractionation, sucrose density gradient sedimentation, immunohistochemistry, anti-SMN immunoprecipitation from nuclear and cytoplasmic extracts BMC cell biology Medium 17640370
2007 Gemin5 physically interacts with ASK1, SEK1, and JNK1, potentiates H2O2-induced activation of these kinases, promotes ASK1 binding to SEK1 and JNK1, and its depletion by RNAi reduces H2O2- and TNFα-induced apoptosis. Gemin5 functions as a scaffold for the ASK1-JNK1 signaling module. Co-immunoprecipitation, RNAi knockdown with kinase activity assays, apoptosis assays Cell death and differentiation Medium 17541429
2008 Gemin5 functions as a down-regulator of both cap-dependent and IRES-driven translation initiation. It binds FMDV and HCV IRES elements, and forms two distinct complexes: a specific IRES-RNP complex and an IRES-independent complex containing eIF4E. Riboproteomics, UV-crosslinking immunoprecipitation, shRNA depletion with in vitro translation assays, pull-down assays Nucleic acids research High 19066202
2009 Gemin5 binds snRNAs via its WD repeat domain, which is both necessary and sufficient for sequence-specific, high-affinity RNA binding. Specific amino acids in a discrete region of the WD repeat domain contact snRNAs, as identified by RNA-mediated hydroxyl radical probing and confirmed by mutagenesis. Deletion analysis, RNA-mediated hydroxyl radical probing, mass spectrometry mapping, site-directed mutagenesis Nature structural & molecular biology High 19377484
2009 Gemin5 directly and specifically associates with the m7G cap structure via its N-terminal WD repeat domain, with two proximal aromatic residues in the WD repeat region critical for m7G association. Cap-affinity chromatography, UV crosslinking to radiolabeled cap, deletion analysis, site-directed mutagenesis PloS one High 19750007
2010 Gemin5 delivers pre-snRNA precursors (pre-snRNAs) as substrates to the SMN complex for Sm core assembly and processing. A transient pre-snRNA-Gemin5 intermediate accumulates upon protein synthesis inhibition, and pre-snRNA 3' sequences enhance snRNP biogenesis. High-throughput screening for SMN complex inhibitors, formaldehyde crosslinking riboproteomics, high-throughput sequencing of the Gemin5-pre-snRNA intermediate Molecular cell High 20513430
2010 In Drosophila, Gemin5 (Rigor mortis ortholog) colocalizes with SMN in cytoplasmic U bodies, which are associated with P bodies, implicating the SMN complex and Gemin5 in snRNP assembly at discrete cytoplasmic granules. Immunofluorescence co-localization in Drosophila egg chambers Experimental cell research Medium 20452345
2012 The C-terminal region of Gemin5, but not the N-terminal region, binds viral IRES elements preferentially via a hairpin flanked by A/U/C-rich sequences and impairs IRES-dependent translation. Addition of purified Gemin5 induces specific protection of IRES residues and competes with PTB-induced conformational changes. RNA-binding assays with purified proteins, SHAPE analysis, translation assays Nucleic acids research High 23221641
2012 Gemin5 is cleaved by FMDV L protease in infected cells but not by other picornavirus proteases, yielding stable fragments p85 and p57. A novel L protease recognition motif (R)(R/K)(L/A)(R) was defined by mutagenesis. Infection assays, viral protease expression, in silico search, mutagenesis Nucleic acids research Medium 22362733
2014 The C-terminal region of Gemin5 contains two non-canonical bipartite RNA-binding sites (RBS1, aa 1297–1412; RBS2, aa 1383–1508). RBS2, despite lower RNA-binding affinity, is the minimal element sufficient to repress IRES-dependent translation when expressed in cells. RNA-binding affinity assays with purified proteins, NMR structure in solution, translation reporter assays in cells Nucleic acids research High 24598255
2015 Gemin5 binds directly to sequence and structural elements in the SMN mRNA 3'-UTR resembling the snRNP code, activating SMN translation. SMN protein reciprocally regulates the mRNA-binding activity of Gemin5, creating a feedback autoregulatory loop. In vitro RNA-binding assays, RIP (RNA immunoprecipitation), polysome profiling, Gemin5 depletion with translation readout The Journal of biological chemistry High 25911097
2016 The WD40 domain of Gemin5 is necessary and sufficient to bind the Sm site of pre-snRNAs. Crystal structures of the WD40 domain in complex with the Sm site and m7G cap of pre-snRNA reveal two distinct binding sites with base-specific interactions. Gemin5 can escort truncated U1 pre-snRNAs for disposal. Crystal structure determination, ITC, mutagenesis Genes & development High 27881600
2016 The N-terminal half of Gemin5 comprises two juxtaposed seven-bladed WD40 repeat domains that form a contiguous RNA-binding surface. Base-stacking interactions involving four aromatic residues and hydrogen bonding by a pair of arginines are crucial for specific recognition of the Sm site sequence. Crystal structure determination, structural and biochemical analyses, mutagenesis Genes & development High 27881601
2016 Gemin5 sediments with the ribosome fraction and its N-terminal domain directly binds ribosome particles. Ribosomal proteins L3 and L4 bind directly to Gemin5. Mutants F381A and Y474A lose ribosome binding. Gemin5 depletion increases, and overexpression decreases, global protein synthesis, and Gemin5 is detected on polysome fractions. Subcellular fractionation, His-Gemin5 pull-down of ribosomes, Co-IP of L3/L4, site-directed mutagenesis, polysome profiling Nucleic acids research High 27507887
2018 In SMN-deficient cells, non-Sm-associated U1 snRNA and U1A accumulate in cytoplasmic granules colocalizing with P bodies. Gemin5 associates more with U1A and P body components under SMN deficiency, and Gemin5 knockdown eliminates these unassembled U1 snRNP granules, indicating Gemin5 promotes unassembled U1 snRNA disposal. Immunoprecipitation, immunofluorescence co-localization, Gemin5 knockdown with snRNA level measurement FEBS letters Medium 29537490
2018 The RBS1 domain of Gemin5 C-terminus predominantly recognizes the Gemin5 mRNA itself. RBS1 physically interacts with a thermodynamically stable stem-loop in the Gemin5 mRNA, upregulating its translation and counteracting the global translation-repressing activity of full-length Gemin5. CLIP, RNA immunoprecipitation, RNA-binding assays, translation reporter assays, stem-loop mutagenesis Nucleic acids research High 29771365
2020 The middle region of Gemin5 contains an extended tetratricopeptide (TPR)-like domain that self-assembles into a canoe-shaped dimer. This dimerization module mediates interaction between the viral-induced cleavage fragment p85 and full-length Gemin5, anchoring splicing and translation members. A point mutation in the TPR-like domain disrupts dimerization and abrogates p85-induced translation enhancement. Crystal structure determination, mutagenesis, Co-IP in living cells, translation assays Nucleic acids research High 31799608
2020 The PXSS motif within the RBS1 domain of Gemin5 is critical for RNA binding and translation stimulation. Substitutions at P1297 or S1299S1300 drastically reduce binding to the SL1 stem-loop of Gemin5 mRNA and abolish translation enhancement in cells. RBS1 footprint assays, gel-shift assays, mutagenesis, translation reporter assays in cells RNA biology Medium 32476560
2021 Loss-of-function mutations in GEMIN5 perturb subcellular distribution, stability, and expression of GEMIN5 and its interacting partners in patient iPSC-derived neurons, and disrupt snRNP complex assembly. Knock-down of the Drosophila homolog rigor mortis causes developmental defects, motor dysfunction, and reduced lifespan. Patient iPSC-derived neuron studies, Western blotting, snRNP assembly assays, Drosophila knockdown with behavioral phenotyping Nature communications High 33963192
2021 The RBS1 domain of Gemin5 is intrinsically unstructured and recognizes RNA via conserved aromatic and arginine residues through π-π interactions; net charge and π-amino acid density are key determinants of RNA binding by this non-canonical domain. Solution NMR, mutational analysis, RNA-binding assays RNA biology High 34424823
2022 Clinical variants in Gemin5's TPR-like dimerization module disrupt protein dimerization and abolish ribosome association, while an RBS1 variant confers protein instability. All disease mutants are defective in interaction with translation and RNA-driven protein networks. Structural analysis, protein dimerization assays, ribosome binding assays, interactome analysis by mass spectrometry Life science alliance Medium 35393353
2022 The Gemin5 C-terminal region adopts a homodecamer architecture (dimer of pentamers). The intact pentamer/decamer is required for binding cognate RNA ligands and regulating mRNA translation; high-order assembly is driven by pentamerization enabling coordinated RNA binding. Cryo-EM/crystal structure determination, mutagenesis, RNA-binding assays, translation assays Nature communications High 36056043
2022 Gemin5 promotes polysome association of ribosomal mRNAs (bearing 5'TOP motifs) and histone mRNAs (bearing 3' histone stem-loop structures), stimulating their translation. Disruption of the TOP motif impairs Gemin5-RNA interaction. Genome-wide polysome profiling, RNA immunoprecipitation, translation reporter assays with TOP motif mutagenesis Cellular and molecular life sciences Medium 35987821
2022 Phosphorylation at T897 in the TPR-like dimerization domain modulates Gemin5's protein interaction network and translation regulatory activity. T897A mutation strongly reduces association with translation-related cellular proteins, while phosphomimetic T897E partially rescues translation activity. Mass spectrometry identification of phosphoresidues, mutagenesis (Ala and Glu substitutions), translation assays, MS-based interactome analysis, structural modeling Computational and structural biotechnology journal Medium 36420152
2023 SMN binds directly to the C-terminus of Gemin5 via its Tudor domain, regulates GEMIN5 expression, and acts as a genetic suppressor of GEMIN5-mediated neurodegeneration in vivo. SMN upregulation (gene therapy or Nusinersen) rescues defective snRNP biogenesis and alternative splicing caused by GEMIN5 loss. Co-IP mapping of SMN-Gemin5 interaction, SMN Tudor domain mutagenesis, gene therapy/ASO rescue in iPSC neurons and fly model, snRNP assembly assays Acta neuropathologica Medium 37369805
2024 Gemin5 oligomerization (via its WD40 and TPR dimerization domains) is required for ribosome association and translation regulation; association with SMN, Gemin2, and Gemin4 is determined by the dimerization module alone. Loss of oligomerization does not affect cytoplasmic localization. Interactome analysis of oligomerization-proficient/deficient constructs, polysome fractionation, ribosome binding assays, Co-IP Cell death discovery Medium 38942768
2024 GEMIN5 was identified as a novel functional interactor of HSPA8 in colorectal cancer; the HSPA8-GEMIN5 complex mediates splicing-translation coupling, and disruption of this complex by a natural compound causes aberrant splicing of ribosomal protein-coding genes and impaired ribosome biogenesis. Chemical proteomics, CETSA, SPR, Co-IP, GST pull-down, SPIDER proximity labeling Journal of experimental & clinical cancer research Medium 41545989
2025 Phosphoresidues Ser/Thr 847 and 852-854 in the dimerization domain regulate ribosome binding and cap-dependent protein synthesis; non-phosphorylatable substitutions reduce protein stability and ribosome association, while dsRNA-mimic signaling (eIF2α phosphorylation) enhances Gemin5 binding to cognate RNA. Mutagenesis (non-phosphorylatable and phosphomimetic substitutions), ribosome binding assays, translation assays, subcellular fractionation RNA biology Medium 40734649
2025 Gemin5 does not bind the Sm site of U7 snRNA (which differs from spliceosomal snRNA Sm sites), allowing alternative proteins (PTBP1, IGF2BP3, hnRNP A1) to substitute for Gemin5 in U7-specific Sm ring assembly. Affinity pulldown from mammalian extracts with U7 snRNA, protein identification by mass spectrometry RNA Medium 40592581

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. The Journal of biological chemistry 136 11714716
2006 The Gemin5 protein of the SMN complex identifies snRNAs. Molecular cell 132 16857593
2010 Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis. Molecular cell 116 20513430
2008 A novel role for Gemin5 in mRNA translation. Nucleic acids research 94 19066202
2009 Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains. Nature structural & molecular biology 86 19377484
2016 Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly. Genes & development 61 27881600
2012 Gemin5 promotes IRES interaction and translation control through its C-terminal region. Nucleic acids research 59 23221641
2016 The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation. Nucleic acids research 55 27507887
2012 Gemin5 proteolysis reveals a novel motif to identify L protease targets. Nucleic acids research 52 22362733
2014 Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation. Nucleic acids research 47 24598255
2009 Identification of gemin5 as a novel 7-methylguanosine cap-binding protein. PloS one 45 19750007
2016 Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5. Genes & development 44 27881601
2021 Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder. Nature communications 43 33963192
2007 Absence of gemin5 from SMN complexes in nuclear Cajal bodies. BMC cell biology 41 17640370
2006 Quantitative proteomics identifies Gemin5, a scaffolding protein involved in ribonucleoprotein assembly, as a novel partner for eukaryotic initiation factor 4E. Journal of proteome research 41 16739988
2010 Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components of U bodies. Experimental cell research 37 20452345
2015 Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate SMN Expression. The Journal of biological chemistry 36 25911097
2008 Alterations in Gemin5 expression contribute to alternative mRNA splicing patterns and tumor cell motility. Cancer research 34 18245461
2020 Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control. International journal of molecular sciences 32 32485878
2015 Gemin5: A Multitasking RNA-Binding Protein Involved in Translation Control. Biomolecules 31 25898402
2018 The landscape of the non-canonical RNA-binding site of Gemin5 unveils a feedback loop counteracting the negative effect on translation. Nucleic acids research 27 29771365
2020 Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control. Nucleic acids research 24 31799608
2021 Pathogenic variants in the survival of motor neurons complex gene GEMIN5 cause cerebellar atrophy. Clinical genetics 21 34569062
2007 Positive regulation of ASK1-mediated c-Jun NH(2)-terminal kinase signaling pathway by the WD-repeat protein Gemin5. Cell death and differentiation 20 17541429
2019 Impact of RNA-Protein Interaction Modes on Translation Control: The Versatile Multidomain Protein Gemin5. BioEssays : news and reviews in molecular, cellular and developmental biology 19 30919488
2022 Autosomal Recessive Cerebellar Atrophy and Spastic Ataxia in Patients With Pathogenic Biallelic Variants in GEMIN5. Frontiers in cell and developmental biology 17 35295849
2022 Functional and structural deficiencies of Gemin5 variants associated with neurological disorders. Life science alliance 14 35393353
2020 RNA-protein coevolution study of Gemin5 uncovers the role of the PXSS motif of RBS1 domain for RNA binding. RNA biology 13 32476560
2022 Gemin5-dependent RNA association with polysomes enables selective translation of ribosomal and histone mRNAs. Cellular and molecular life sciences : CMLS 11 35987821
2022 Structural basis for Gemin5 decamer-mediated mRNA binding. Nature communications 11 36056043
2021 The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues. RNA biology 11 34424823
2016 The right pick: structural basis of snRNA selection by Gemin5. Genes & development 10 27881598
2024 Mutations of GEMIN5 are associated with coenzyme Q10 deficiency: long-term follow-up after treatment. European journal of human genetics : EJHG 9 38316953
2018 Gemin5 plays a role in unassembled-U1 snRNA disposal in SMN-deficient cells. FEBS letters 9 29537490
2023 SMN regulates GEMIN5 expression and acts as a modifier of GEMIN5-mediated neurodegeneration. Acta neuropathologica 8 37369805
2021 Mutation of Gemin5 Causes Defective Hematopoietic Stem/Progenitor Cells Proliferation in Zebrafish Embryonic Hematopoiesis. Frontiers in cell and developmental biology 8 33996826
2023 A Biallelic Truncating Variant in the TPR Domain of GEMIN5 Associated with Intellectual Disability and Cerebral Atrophy. Genes 7 36980979
2022 Phosphorylation of T897 in the dimerization domain of Gemin5 modulates protein interactions and translation regulation. Computational and structural biotechnology journal 6 36420152
2024 Expanding the clinical phenotype and genetic spectrum of GEMIN5 disorders: Early-infantile developmental and epileptic encephalopathies. Brain and behavior 5 38773790
2023 Novel compound heterozygous mutation and phenotype in the tetratricopeptide repeat-like domain of the GEMIN5 gene in two Chinese families. Journal of human genetics 5 37479787
2024 Oligomerization regulates the interaction of Gemin5 with members of the SMN complex and the translation machinery. Cell death discovery 4 38942768
2024 Alternative splicing events driven by altered levels of GEMIN5 undergo translation. RNA biology 4 39194147
2025 GEMIN5 and neurodevelopmental diseases: From functional insights to disease perception. Neural regeneration research 3 39819844
2025 Understanding GEMIN5 Interactions: From Structural and Functional Insights to Selective Translation. Wiley interdisciplinary reviews. RNA 3 40176294
2024 Function and dysfunction of GEMIN5: understanding a novel neurodevelopmental disorder. Neural regeneration research 3 38526274
2024 Understanding the Role of the SMN Complex Component GEMIN5 and Its Functional Relationship with Demethylase KDM6B in the Flunarizine-Mediated Neuroprotection of Motor Neuron Disease Spinal Muscular Atrophy. International journal of molecular sciences 2 39337533
2019 Regulated expression of Gemin5, Xrn1, Cpeb and Stau1 in the uterus and ovaries after superovulation and the effect of exogenous estradiol and leptin in rodents. Molecular biology reports 1 30689188
2026 Disruption of HSPA8-GEMIN5 interaction suppresses colorectal cancer by impaired splicing-translation coupling-mediated proteostasis imbalance. Journal of experimental & clinical cancer research : CR 0 41545989
2025 Proteins that recognize unique features of U7 snRNA and may substitute for Gemin5 in the assembly of U7-specific Sm ring. RNA (New York, N.Y.) 0 40592581
2025 Impact of Gemin5 in protein synthesis: phosphoresidues of the dimerization domain regulate ribosome binding. RNA biology 0 40734649
2025 N7-Methylguanine Modification of SHMT2 Mediated by GEMIN5 Inhibits Cell Ferroptosis of Colorectal Cancer Cells. Journal of biochemical and molecular toxicology 0 41416630
2024 Corrigendum: Mutation of Gemin5 causes defective hematopoietic stem/progenitor cells proliferation in zebrafish embryonic hematopoiesis. Frontiers in cell and developmental biology 0 38655064