Affinage

EIF4G3

Eukaryotic translation initiation factor 4 gamma 3 · UniProt O43432

Round 2 corrected
Length
1585 aa
Mass
176.7 kDa
Annotated
2026-04-28
52 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EIF4G3 (eIF4GII) is a scaffold subunit of the eIF4F translation initiation complex that bridges cap-bound eIF4E, the RNA helicase eIF4A, the 40S-recruiting factor eIF3, the poly(A)-binding protein PABP, and the eIF4E kinase Mnk1, thereby coupling 5′-cap recognition and 3′-poly(A) tail circularization to ribosome loading (PMID:9418880, PMID:9857202, PMID:9878069). Although broadly redundant with its paralog eIF4GI for bulk translation, eIF4GII is selectively recruited to the cap during erythroid differentiation, is phosphorylated by CaMKI at Ser1156 to promote cap-dependent translation and dendritic spine formation in hippocampal neurons, and is genetically required in mouse spermatocytes for translational activation of HSPA2 mRNA and completion of meiosis (PMID:15143184, PMID:22514323, PMID:20430745). Picornaviral 2A proteases cleave eIF4GII at a specific site (PLLNV699↓GSR), and its delayed cleavage relative to eIF4GI is rate-limiting for host translation shutoff during rhinovirus infection (PMID:12663812, PMID:10074204). EIF4G3 expression is transcriptionally controlled by DEAF1 and post-transcriptionally repressed by miR-520c-3p and miR-375; its downregulation reduces global translation, promotes senescence, and suppresses tumor xenograft growth (PMID:22923498, PMID:24497838, PMID:34194495).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1998 High

    Identification of eIF4GII as a second mammalian eIF4G isoform established that the eIF4F scaffold function is shared between two paralogs capable of independently assembling the cap-binding complex with eIF4E, eIF4A, eIF3, and PABP.

    Evidence Far-Western, co-IP, cap affinity chromatography, in vitro translation rescue in HeLa cells and reticulocyte lysate; PABP interaction mapped via deletion analysis

    PMID:9418880 PMID:9857202

    Open questions at the time
    • Whether eIF4GI and eIF4GII have distinct mRNA-selective roles was unknown
    • Structural basis of eIF4GII scaffold assembly not determined
  2. 1999 High

    Kinetic studies of picornavirus infections revealed that eIF4GII cleavage—not eIF4GI cleavage—is the rate-limiting step for host translation shutoff, demonstrating that eIF4GII alone can sustain cap-dependent translation.

    Evidence Western blot kinetics of eIF4GI/II cleavage correlated with metabolic labeling during poliovirus and HRV-14 infection of HeLa cells

    PMID:10074204 PMID:9736694

    Open questions at the time
    • Exact cleavage site in eIF4GII was not yet mapped
    • Whether eIF4GII resistance reflects sequence divergence or structural protection was unclear
  3. 1999 High

    Demonstration that Mnk1 docks on the C-terminus of both eIF4GI and eIF4GII to phosphorylate eIF4E positioned the eIF4G scaffold as a signaling platform integrating MAPK/p38 input into translation.

    Evidence Co-IP with dominant-negative and activated Mnk1 mutants

    PMID:9878069

    Open questions at the time
    • Whether Mnk1 preferentially utilizes eIF4GII versus eIF4GI in specific contexts was not tested
  4. 2003 High

    Biochemical identification of the HRV2 2Apro cleavage site at PLLNV699↓GSR in eIF4GII resolved the molecular basis of differential protease sensitivity between the two paralogs.

    Evidence In vitro cleavage with recombinant 2Apro followed by N-terminal sequencing of cleavage fragments

    PMID:12663812

    Open questions at the time
    • Structural determinants governing slower cleavage kinetics of eIF4GII versus eIF4GI not resolved
  5. 2004 Medium

    Selective recruitment of eIF4GII, but not eIF4GI, to the cap structure during thrombopoietin-induced erythroid differentiation provided the first evidence that the two paralogs fulfill non-redundant physiological roles.

    Evidence Cap affinity chromatography from differentiating UT-7 cells with Western blot for eIF4GI/II and 4E-BP1

    PMID:15143184

    Open questions at the time
    • Molecular basis of selective eIF4GII recruitment unknown
    • Target mRNAs preferentially translated by eIF4GII in this context not identified
  6. 2006 Medium

    Differential cleavage experiments revealed that eIF4GII is preferentially required for ongoing/reinitiation translation of pre-existing mRNAs (including HSP70), whereas eIF4GI supports de novo translation of newly exported mRNAs.

    Evidence Electroporation of EMCV-IRES-2Apro mRNA into HeLa and BHK-21 cells with luciferase reporters and polysome run-off

    PMID:16959778

    Open questions at the time
    • Genome-wide identification of eIF4GII-dependent mRNAs not performed
    • Whether this division of labor holds outside picornavirus-cleavage conditions is unknown
  7. 2010 High

    Genetic loss of Eif4g3 in mouse spermatocytes caused meiotic arrest at G2/MI by failing to translate HSPA2, a chaperone required for CDK1 activation, establishing eIF4GII as an essential translational regulator of mammalian meiosis.

    Evidence ENU mutagenesis (repro8 allele), positional cloning, histology, immunofluorescence, Western blot, CDK1 kinase assay in mouse testis

    PMID:20430745

    Open questions at the time
    • Whether eIF4GII recognizes specific cis-elements in Hspa2 mRNA is unknown
    • Full spectrum of eIF4GII-dependent mRNAs in spermatocytes not catalogued
  8. 2012 High

    CaMKI-mediated phosphorylation of eIF4GII at Ser1156 in hippocampal neurons was shown to enhance eIF4GII recruitment to the cap and promote dendritic spine formation, linking activity-dependent signaling to selective eIF4GII-driven translation in neurons.

    Evidence In vitro kinase assay with S1156A mutant, cap affinity purification, bicistronic reporter, RNAi knockdown with confocal spine imaging in hippocampal neurons

    PMID:22514323

    Open questions at the time
    • Neuronal mRNAs selectively translated via phospho-S1156 eIF4GII not identified
    • Whether this phosphorylation event is relevant in vivo (learning/memory paradigms) is untested
  9. 2012 Medium

    Parallel studies revealed that eIF4GII expression is transcriptionally regulated by DEAF1 in lymph node stromal cells and that multiple N-terminally extended eIF4GII isoforms generated from alternative promoters and a CUG start codon have distinct translational rescue activities.

    Evidence qRT-PCR, siRNA, polysome profiling in LNSCs; 5′-RACE, isoform overexpression rescue of double-knockdown cells with metabolic labeling

    PMID:22909319 PMID:22923498

    Open questions at the time
    • Physiological significance of individual N-terminal isoforms in specific tissues not established
    • Whether DEAF1-dependent regulation of eIF4GII contributes to autoimmune phenotypes remains correlative
  10. 2014 Medium

    Post-transcriptional repression of EIF4G3 by miR-520c-3p was shown to reduce global translation, promote senescence, and suppress lymphoma xenograft growth, implicating eIF4GII as a rate-limiting translation factor for cell proliferation.

    Evidence 3′-UTR luciferase reporter, siRNA knockdown, xenograft tumor assay in diffuse large B-cell lymphoma model

    PMID:24497838

    Open questions at the time
    • Whether eIF4GII loss triggers senescence through a specific mRNA target or globally reduced translation is unresolved
  11. 2018 Medium

    Unexpected nuclear localization of EIF4G3 in mouse spermatocytes, particularly at the XY body, raised the possibility that eIF4GII has non-cytoplasmic roles during meiotic prophase.

    Evidence Immunofluorescence with confocal microscopy and co-localization with γH2AX and BRCA1 in mouse spermatocyte spreads

    PMID:29161344

    Open questions at the time
    • Functional significance of XY body localization not demonstrated
    • Whether nuclear eIF4GII has any translation-independent function is unknown
    • Biochemical validation of nuclear localization (fractionation controls) limited

Open questions

Synthesis pass · forward-looking unresolved questions
  • The mRNA-selective mechanism by which eIF4GII controls translation of specific targets (e.g. HSPA2, dendritic mRNAs) remains undefined—no cis-regulatory elements, RNA-binding partners, or structural features distinguishing eIF4GII from eIF4GI target selection have been identified.
  • No genome-wide identification of eIF4GII-dependent translatome in any tissue
  • No high-resolution structure of eIF4GII or eIF4GII-specific domains
  • Mechanism of isoform-selective cap recruitment is unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0045182 translation regulator activity 5 GO:0060090 molecular adaptor activity 2 GO:0003723 RNA binding 1
Localization
GO:0005829 cytosol 3 GO:0005634 nucleus 1
Pathway
R-HSA-392499 Metabolism of proteins 6 R-HSA-168256 Immune System 5 R-HSA-1474165 Reproduction 2
Partners
CAMK1EIF3AEIF4A1EIF4EMKNK1PABPC1
Complex memberships
eIF4F

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 eIF4GII (encoded by EIF4G3) was identified as a functional homolog of eIF4GI in mammals, sharing 46% amino acid identity. Far-Western analysis and co-immunoprecipitation demonstrated that eIF4GII directly interacts with eIF4E, eIF4A, and eIF3, and exists in a cap-binding complex with eIF4E in HeLa cells. eIF4GII restores cap-dependent translation in reticulocyte lysate depleted of eIF4G by rhinovirus 2A protease cleavage, and is cleaved upon picornavirus infection. Far-Western analysis, co-immunoprecipitation, cap affinity chromatography, in vitro translation rescue assay Molecular and cellular biology High 9418880
1998 Proteolysis of eIF4GII, but not eIF4GI alone, coincides with the shutoff of host cell protein synthesis after poliovirus infection. Cleavage of both eIF4GI and eIF4GII is required for complete inhibition of host translation; eIF4GII is more resistant to poliovirus-mediated cleavage than eIF4GI. Western blot analysis of eIF4GI/II integrity during poliovirus infection; metabolic labeling to measure protein synthesis; use of virus replication inhibitors Proceedings of the National Academy of Sciences of the United States of America High 9736694
1998 eIF4GII contains a 29-amino-acid sequence in its N-terminal region that is nearly identical to that of eIF4GI, and the full-length eIF4GII binds poly(A)-binding protein (PABP) via this site (specifically via RRM1 and RRM2 of PABP). This interaction implicates eIF4GII in poly(A)-dependent translation. Co-immunoprecipitation, deletion analysis, in vitro translation assay with deadenylated vs. polyadenylated mRNA The EMBO journal High 9857202
1999 eIF4GII cleavage is the rate-limiting step in the shutoff of host protein synthesis after human rhinovirus 14 (HRV-14) infection. eIF4GI is cleaved early but host translation persists until eIF4GII is substantially cleaved (~6 h post-infection), demonstrating that eIF4GII cleavage correlates with translational inhibition. Western blot analysis of eIF4GI/II cleavage kinetics; metabolic labeling of protein synthesis in HRV-14-infected HeLa cells Journal of virology High 10074204
1999 Mnk1 kinase associates with the eIF4F complex via interaction with the C-terminal region of eIF4G (both eIF4GI and eIF4GII), providing a docking site for Mnk1 to phosphorylate eIF4E at Ser209. Co-immunoprecipitation, in vitro binding assays, dominant-negative and activated Mnk1 mutants The EMBO journal High 9878069
2001 The FMDV IRES interacts with eIF4GII, and the RNA determinants for this interaction are shared with eIF4GI. The C-terminal fragment of eIF4GII generated by Lb protease binds the FMDV IRES as efficiently as intact eIF4GII, indicating the IRES-binding domain resides in the C-terminal portion. eIF4G-IRES interaction is the limiting factor for IRES activity. UV crosslinking, competition experiments, bicistronic reporter assays in transfected cells, protease cleavage RNA (New York, N.Y.) Medium 11565745
2002 HIV-1 protease cleaves eIF4GI but not eIF4GII in vitro and in cell extracts, demonstrating differential susceptibility of the two isoforms to this viral protease. Cleavage of eIF4GI by HIV-1 protease impairs both cap-dependent and IRES-containing RNA translation (except HCV IRES), in contrast to picornaviral proteases. In vitro protease assay with cell extracts and rabbit reticulocyte lysate; HIV-1 protease inhibitor (palinavir) as control; in vitro translation assays Journal of molecular biology Medium 12054764
2002 HRV2 2A proteinase directly cleaves both eIF4GI and eIF4GII without requiring activation of a cellular proteinase, as demonstrated using a thermosensitive 2Apro mutant in temperature-shift experiments with HeLa cell extracts. Temperature-shift experiments with thermosensitive HRV2 2Apro mutant in cytoplasmic cell extracts; Western blot FEBS letters Medium 12123803
2003 The HRV2 2Apro cleavage site in eIF4GII was identified in vitro as PLLNV(699)*GSR, located seven amino acids C-terminal to the analogous cleavage site in eIF4GI (LSTR681*GPP), demonstrating that the two isoforms have distinct but nearby cleavage sites for the same viral protease. In vitro cleavage assay with recombinant HRV2 2Apro, N-terminal sequencing of cleavage fragments Journal of virology High 12663812
2004 eIF4GII, but not eIF4GI, is selectively recruited to capped mRNA at the onset of erythroid cell differentiation induced by thrombopoietin. This selective recruitment is coincident with strong phosphorylation of eIF4E and release of 4E-BP1 from the cap structure, providing the first evidence that eIF4GI and eIF4GII fulfill distinct roles in mammalian cells. Cap affinity chromatography from differentiating cells, Western blot for eIF4GI/II, 4E-BP1, and phospho-eIF4E Molecular and cellular biology Medium 15143184
2006 Differential cleavage of eIF4GI and eIF4GII by poliovirus 2Apro revealed functionally distinct roles: de novo translation of newly synthesized mRNA depends primarily on eIF4GI integrity, whereas ongoing translation and reinitiation of pre-existing mRNA translation after polysome run-off are more dependent on eIF4GII. Translation of HSP70 mRNA depends more on eIF4GII than eIF4GI. Electroporation of EMCV IRES-2Apro mRNA into HeLa and BHK-21 cells; luciferase reporter assays; polysome run-off experiments The Journal of biological chemistry Medium 16959778
2009 Depletion of eIF4GI or eIF4GII individually only moderately inhibits cellular protein synthesis, while depletion of both together has a slightly greater inhibitory effect. Vaccinia virus (VV) mRNA translation requires eIF4GI/II and eIF4E (cap-dependent), whereas vesicular stomatitis virus (VSV) mRNA translation does not require eIF4GI or eIF4GII despite being capped. siRNA-mediated depletion of eIF4GI and/or eIF4GII in HeLa cells; metabolic labeling; viral protein synthesis assays Journal of molecular biology Medium 19769989
2010 ENU-induced mutation of mouse Eif4g3 (repro8 allele) causes male-limited infertility due to meiotic arrest at the G2/MI transition. EIF4G3 is required for translational control of HSPA2 (a chaperone for CDK1/CDC2A kinase) in spermatocytes: Hspa2 mRNA is present but HSPA2 protein is absent in mutant cells, resulting in dramatically reduced CDK1 kinase activity. This is the first genetic evidence for selective translational control of meiotic exit in mammalian spermatocytes. ENU mutagenesis screen, positional cloning, histology, immunofluorescence, Western blot, kinase activity assay (CDK1), comparison with Hspa2 knockout phenotype Development (Cambridge, England) High 20430745
2001 Both eIF4GI and eIF4GII are cleaved in Jurkat T cells in response to proteasome inhibitors (MG132, lactacystin) and immunosuppressants (FTY720, cyclosporin A) by caspase-8-independent mechanisms. Proteasome inhibitor-induced cleavage of eIF4GI generates a novel fragment lacking the eIF4E-binding capability, distinct from the anti-Fas-induced cleavage pattern. Western blot with anti-peptide antisera specific for eIF4GI and eIF4GII; caspase-8-deficient Jurkat cell line; pharmacological inhibitors FEBS letters Medium 11513883
2012 CaMKI phosphorylates eIF4GII at Ser1156 in an activity-dependent manner in hippocampal neurons. This phosphorylation promotes selective recruitment of eIF4GII (but not eIF4GI) into the eIF4F complex assembled at the mRNA 5' cap, upregulating cap-dependent translation. RNAi knockdown of eIF4GII reduces cap-dependent translation and decreases density of dendritic filopodia and spine formation without affecting dendritic arborization. In vitro CaMKI phosphorylation assay, m7GTP cap affinity purification, bicistronic luciferase reporter, RNAi knockdown in hippocampal neurons, confocal imaging of spine morphology, pharmacological inhibition (STO-609, NMDA receptor blockers) The Journal of neuroscience High 22514323
2012 DEAF1 transcriptionally regulates Eif4g3 expression in lymph node stromal cells (LNSCs). Reduced DEAF1 function (in Deaf1-KO mice, NOD mice, and T1D patients) leads to decreased Eif4g3 transcription and also increased Caspase 3 expression (which degrades eIF4GII protein). Polysome profiling showed that reduced eIF4GII in LNSCs diminishes translation of multiple genes including Anpep. qRT-PCR, siRNA silencing of Deaf1, polysome profiling, Western blot, comparison across Deaf1-KO mice, NOD mice, and T1D patient samples Journal of molecular cell biology Medium 22923498
2012 Multiple isoforms of eIF4GII are generated in mammalian cells via alternative promoters, alternative splicing, and use of a non-canonical CUG initiation codon that extends the N-terminus. The novel N-terminal-extended eIF4GII isoforms rescue translation in eIF4GI/eIF4GII double-knockdown cells as effectively as the eIF4GIf/e isoforms, more robustly than the original eIF4GII, suggesting the eIF4GII N-terminus has a role distinct from eIF4GI in translation initiation factor assembly. RT-PCR, 5' RACE, RNAi knockdown, rescue experiments with overexpression of isoforms, metabolic labeling of translation rates The Biochemical journal Medium 22909319
2013 eIF4GII undergoes novel Cdk1-dependent N-terminal phosphorylation in nocodazole-arrested cells. This phosphorylation, along with eIF2α phosphorylation and polysome disaggregation, contributes to the inhibition of translation observed in nocodazole-arrested cells, which had previously been attributed to mitosis itself. Translation rates do not intrinsically slow during mitosis when cells are synchronized without nocodazole. FACS-synchronized HeLa cells (double thymidine block or RO3306 release), pulse labeling with [35S]-methionine, confocal microscopy of translation factors, polysome analysis, phosphorylation analysis by Western blot Cell cycle (Georgetown, Tex.) Medium 24091728
2014 miR-520c-3p directly targets eIF4GII (EIF4G3) mRNA, repressing its translation. Downregulation of eIF4GII by either miR-520c-3p or siRNA decreases global translation, reduces cell proliferation, promotes cellular senescence, and suppresses tumor growth in xenograft models of diffuse large B-cell lymphoma. miRNA overexpression, siRNA knockdown, luciferase reporter assays (3'UTR targeting), xenograft tumor assay, Western blot, proliferation assays PLoS genetics Medium 24497838
2018 EIF4G3 localizes unexpectedly to the nucleus of mouse spermatocytes, with high enrichment in the XY body (the chromatin domain of transcriptionally silenced sex chromosomes). Many other translation-related proteins also localize to the XY body, suggesting a role for this domain in storing or poising translation complexes before the meiotic division phase. Immunofluorescence, confocal microscopy, subcellular fractionation, co-localization with XY body markers (γH2AX, BRCA1) Biology of reproduction Medium 29161344
2021 EIF4G3 is a direct target of miR-375 in lung squamous cell carcinoma cells. Chidamide treatment upregulates miR-375, which suppresses EIF4G3 mRNA and protein expression. Silencing EIF4G3 independently induces apoptosis and suppresses tumor growth, while inhibition of miR-375 reverses chidamide-induced apoptosis and stemness suppression, confirming EIF4G3 as a functional mediator of the chidamide/radiation response. miRNA microarray, luciferase reporter assay (direct miR-375 target validation), Western blot, siRNA knockdown of EIF4G3, xenograft tumor assay Journal of oncology Medium 34194495

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2861 17081983
2009 Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2592 19239892
1999 eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annual review of biochemistry 1748 10872469
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
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
2006 A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nature biotechnology 1336 16964243
2009 Defining the human deubiquitinating enzyme interaction landscape. Cell 1282 19615732
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
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2007 Large-scale mapping of human protein-protein interactions by mass spectrometry. Molecular systems biology 733 17353931
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
2016 An improved smaller biotin ligase for BioID proximity labeling. Molecular biology of the cell 665 26912792
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
1999 Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. The EMBO journal 538 9878069
1994 Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene 492 8125298
1998 A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. The EMBO journal 487 9857202
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 Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. Journal of proteome research 422 20020773
2005 Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Genome research 409 16344560
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
1999 Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Molecular and cellular biology 406 10022874
1998 Proteolysis of human eukaryotic translation initiation factor eIF4GII, but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection. Proceedings of the National Academy of Sciences of the United States of America 285 9736694
2017 Genome-wide CRISPR screen identifies HNRNPL as a prostate cancer dependency regulating RNA splicing. Proceedings of the National Academy of Sciences of the United States of America 282 28611215
2004 Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. Nature biotechnology 266 15146197
1998 A novel functional human eukaryotic translation initiation factor 4G. Molecular and cellular biology 259 9418880
2001 IRES interaction with translation initiation factors: functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII. RNA (New York, N.Y.) 103 11565745
1999 Eukaryotic initiation factor 4GII (eIF4GII), but not eIF4GI, cleavage correlates with inhibition of host cell protein synthesis after human rhinovirus infection. Journal of virology 101 10074204
2002 In vitro cleavage of eIF4GI but not eIF4GII by HIV-1 protease and its effects on translation in the rabbit reticulocyte lysate system. Journal of molecular biology 64 12054764
2022 Circular RNA EIF4G3 suppresses gastric cancer progression through inhibition of β-catenin by promoting δ-catenin ubiquitin degradation and upregulating SIK1. Molecular cancer 61 35780119
2010 Mutation of Eif4g3, encoding a eukaryotic translation initiation factor, causes male infertility and meiotic arrest of mouse spermatocytes. Development (Cambridge, England) 61 20430745
2013 Phosphorylation of eIF4GII and 4E-BP1 in response to nocodazole treatment: a reappraisal of translation initiation during mitosis. Cell cycle (Georgetown, Tex.) 45 24091728
2006 Differential cleavage of eIF4GI and eIF4GII in mammalian cells. Effects on translation. The Journal of biological chemistry 38 16959778
2014 Down-regulation of eIF4GII by miR-520c-3p represses diffuse large B cell lymphoma development. PLoS genetics 36 24497838
2004 Selective modification of eukaryotic initiation factor 4F (eIF4F) at the onset of cell differentiation: recruitment of eIF4GII and long-lasting phosphorylation of eIF4E. Molecular and cellular biology 36 15143184
2012 Reduced DEAF1 function during type 1 diabetes inhibits translation in lymph node stromal cells by suppressing Eif4g3. Journal of molecular cell biology 34 22923498
2009 Translation of mRNAs from vesicular stomatitis virus and vaccinia virus is differentially blocked in cells with depletion of eIF4GI and/or eIF4GII. Journal of molecular biology 26 19769989
2003 Human rhinovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different. Journal of virology 24 12663812
2018 Nuclear localization of EIF4G3 suggests a role for the XY body in translational regulation during spermatogenesis in mice. Biology of reproduction 22 29161344
2012 Regulation of neuronal mRNA translation by CaM-kinase I phosphorylation of eIF4GII. The Journal of neuroscience : the official journal of the Society for Neuroscience 20 22514323
2012 Multiple isoforms of the translation initiation factor eIF4GII are generated via use of alternative promoters, splice sites and a non-canonical initiation codon. The Biochemical journal 16 22909319
2002 A thermosensitive mutant of HRV2 2A proteinase: evidence for direct cleavage of eIF4GI and eIF4GII. FEBS letters 15 12123803
2009 Visualizing and quantifying the differential cleavages of the eukaryotic translation initiation factors eIF4GI and eIF4GII in the enterovirus-infected cell. Biotechnology and bioengineering 14 19655339
2021 Chidamide and Radiotherapy Synergistically Induce Cell Apoptosis and Suppress Tumor Growth and Cancer Stemness by Regulating the MiR-375-EIF4G3 Axis in Lung Squamous Cell Carcinomas. Journal of oncology 13 34194495
2019 Circ-EIF4G3 promotes the development of gastric cancer by sponging miR-335. Pathology, research and practice 12 31257089
2001 Proteasome inhibitors and immunosuppressive drugs promote the cleavage of eIF4GI and eIF4GII by caspase-8-independent mechanisms in Jurkat T cell lines. FEBS letters 9 11513883
2026 The related EIF4G3 and EIF4G4 initiation factors from Leishmania: dissimilar modes of action during translation revealed by a comparative proteomic approach. Parasites & vectors 0 41776682