Affinage

EIF2S2

Eukaryotic translation initiation factor 2 subunit 2 · UniProt P20042

Length
333 aa
Mass
38.4 kDa
Annotated
2026-06-09
27 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/5 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EIF2S2 (eIF2β) is the β-subunit of the heterotrimeric eIF2 GTPase complex that delivers initiator Met-tRNAi to the 40S ribosome and governs the fidelity of start codon selection (PMID:22851688, PMID:27458202). Its eukaryote-specific N- and C-terminal extensions make the dominant contribution to Met-tRNAi binding affinity within the eIF2 complex (PMID:23193270), and its C-terminal zinc-binding domain (ZBD) contacts the eIF2γ guanine nucleotide-binding interface as a second binding site that promotes Met-tRNAi loading; ZBD mutations such as S264Y disrupt the β–γ interaction, cause Met-tRNAi binding defects, and relax start codon stringency to permit aberrant near-cognate UUG initiation (PMID:38873976, PMID:41460464). The three N-terminal lysine-rich K-box repeats form a platform of three discrete, overlapping binding sites that are competitively occupied by eIF5-CTD, eIF2Bε, and 5MP1 with mutually reduced affinities; the K-boxes promote mRNA binding to the 40S subunit, an activity reversed by eIF5-CTD, which switches the pre-initiation complex from an open to a closed state to drive AUG recognition and eIF1 release (PMID:22813744, PMID:22851688, PMID:40670154). eIF2β thereby coordinates the GDP/GTP recycling cycle: eIF5-CTD acts as a GDP-dissociation inhibitor on eIF2•GDP, eIF2Bε contacts eIF2β via residue W699 to catalyze nucleotide exchange and accelerate eIF5 dissociation, and a specific eIF2β mutation that blocks eIF5 GDI activity increases the GDP off-rate and impairs GCN4 translational induction during amino acid starvation (PMID:17526738, PMID:27458202, PMID:40670154). eIF2β is regulated by phosphorylation: CK2 directly binds both CK2α and CK2β subunits and phosphorylates eIF2β at Ser2 and Ser67, and phosphomimetic substitutions increase eIF2β's affinities for eIF5, eIF2Bε, and 5MP1; PP1 docks via an RVxF motif to dephosphorylate the same sites (PMID:12901717, PMID:16225457, PMID:16987104, PMID:40670154). Beyond canonical initiation, eIF2β participates in DAP5-dependent cap-independent (IRES) translation (PMID:25779044), regulates SMAD4 post-translationally in cervical cancer cells (PMID:39370734), and is required for early embryonic viability and germ cell development in mice, where its loss disrupts mitochondrial function and triggers the integrated stress response and apoptosis (PMID:39044637, PMID:19168544). In Drosophila neurons, eIF2β acts in a mitochondria–eIF2β axis whose dysregulation produces autophagic defects (PMID:41587080).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2001 High

    Established the division of labor among eIF2 subunits, showing eIF2β contributes to the catalytic core rather than to eIF2B recognition.

    Evidence Reconstituted purified yeast eIF2βγ complex with steady-state kinetic and in vitro 43S assembly assays

    PMID:11042214

    Open questions at the time
    • Did not map which eIF2β surfaces contact eIF2B
    • Used a yeast system without confirming human subunit equivalence
  2. 2002 High

    Defined the two-domain architecture (DNA-binding-like N-terminal domain and a Cys-coordinated zinc-binding C-terminal motif) later used to interpret eukaryotic eIF2β.

    Evidence Multidimensional NMR of recombinant archaeal aIF2β

    PMID:11980477

    Open questions at the time
    • Archaeal homolog lacks the eukaryote-specific K-box extensions
    • Functional roles of each domain not tested here
  3. 2003 High

    Identified eIF2β as a direct CK2 binding partner and substrate, linking translation initiation to a constitutive kinase.

    Evidence Co-IP in HeLa, SPR, in vitro kinase assays with domain truncations

    PMID:12901717

    Open questions at the time
    • Specific phosphoacceptor residues not pinpointed in this study
    • Functional consequence of phosphorylation untested
  4. 2005 Medium

    Mapped the eIF2β–CK2α interface and showed eIF2β reciprocally modulates CK2α catalytic activity.

    Evidence SPR, kinase activity assays, gel filtration with mutant CK2α/eIF2β

    PMID:16335529

    Open questions at the time
    • Single lab
    • Physiological relevance of CK2α stimulation in cells unaddressed
  5. 2006 High

    Defined CK2 phosphosites Ser2/Ser67 in vivo and demonstrated the eIF2β N-terminus is functionally essential for eIF5 binding and protein synthesis.

    Evidence CK2 inhibitors, kinase-dead CK2α, phosphosite/truncation mutants, translation reporters in HeLa

    PMID:16225457

    Open questions at the time
    • Mechanistic link between phosphorylation and partner affinity not yet quantified
    • S2/67A did not affect trimer assembly or eIF5 binding, leaving the rate-limiting step unclear
  6. 2006 High

    Identified PP1 as the phosphatase acting on eIF2β via an RVxF docking motif, establishing reversible phosphocontrol of the subunit.

    Evidence Reciprocal Co-IP, pull-downs with purified components, RVxF mutagenesis, phosphatase assays

    PMID:16987104

    Open questions at the time
    • Did not resolve how PP1 docking is regulated
    • RVxF mutation did not alter basal translation, leaving in-cell impact ambiguous
  7. 2007 High

    Distinguished the eIF2Bε contacts to eIF2β (W699) from those to eIF2γ, clarifying how the GEF engages the substrate for nucleotide exchange.

    Evidence Surface-residue mutagenesis, yeast lethality complementation, subunit binding and GCN4 GEF assays

    PMID:17526738

    Open questions at the time
    • Structural geometry of the dual contacts not resolved
    • Relative kinetic contribution of each contact unquantified
  8. 2012 High

    Showed eIF5-CTD and eIF1 bind overlapping eIF2β surfaces and that this interplay drives the open-to-closed PIC transition required for AUG selection.

    Evidence NMR mapping, eIF5-CTD mutagenesis, yeast complementation, PIC assembly assays

    PMID:22813744

    Open questions at the time
    • Did not capture the closed-state structure directly
    • Order of eIF1 release relative to GTP hydrolysis not resolved
  9. 2012 High

    Assigned a positive mRNA-recruitment function to the eIF2β K-boxes, antagonized by eIF5-CTD to prime the ribosome for start codon recognition.

    Evidence In vitro 40S mRNA binding with purified factors, yeast genetic epistasis, GCN4 fidelity reporters

    PMID:22851688

    Open questions at the time
    • Molecular basis of K-box mRNA contact not structurally defined
    • Generality to specific mRNAs untested
  10. 2012 High

    Demonstrated that the eukaryote-specific eIF2β extensions are the dominant determinant of Met-tRNAi binding affinity.

    Evidence Chimeric eIF2 complexes, tRNA binding assays, SAXS

    PMID:23193270

    Open questions at the time
    • Used yeast/archaeal chimeras rather than full native complexes
    • Did not localize the tRNA contact residues
  11. 2016 High

    Showed an eIF2β mutation can selectively block eIF5 GDI function, defining eIF2β's role in stabilizing GDP and tuning the stress response.

    Evidence Fluorescent nucleotide and tRNA binding, eIF5 GDI assays, genetics and GCN4 reporters with purified eIF2

    PMID:27458202

    Open questions at the time
    • The mutated residue's normal contribution to the GDI interface not structurally mapped
    • Conservation in human eIF2β not tested
  12. 2017 Medium

    Linked the eIF2β polylysine K-boxes to nuclear/nucleolar trafficking and showed their deletion is dominant-negative for translation and cell cycle progression.

    Evidence Tet-inducible eIF2βΔ3K in HEK293, translation reporters, flow cytometry, confocal localization

    PMID:28692326

    Open questions at the time
    • Functional significance of nucleolar localization unclear
    • Dominant-negative effects may reflect titration of partners rather than a native nuclear role
  13. 2024 Medium

    Identified a second eIF2β ZBD–eIF2γ contact at the nucleotide-binding interface that promotes Met-tRNAi binding, with intragenic suppression validating the interaction.

    Evidence Yeast suppressor genetics, in vitro subunit binding, Met-tRNAi binding and GTPase assays

    PMID:38873976

    Open questions at the time
    • No co-crystal of the ZBD–γ interface
    • Single lab; human relevance inferred
  14. 2024 Medium

    Revealed a non-canonical role: eIF2S2 binds the SMAD4 MH-1 domain and post-translationally downregulates SMAD4, dampening antiproliferative gene expression in cervical cancer.

    Evidence Co-IP, BiFC, siRNA/overexpression, qRT-PCR, luciferase promoter assays

    PMID:39370734

    Open questions at the time
    • Mechanism of SMAD4 destabilization (degradation route) undefined
    • Single cell-line context
  15. 2024 Medium

    Defined eIF2β as essential for oogenesis, with loss disrupting meiotic recombination, mitochondrial function, and triggering the integrated stress response and apoptosis.

    Evidence Premeiotic conditional Eif2s2 knockout in mice with protein, mitochondrial, and apoptosis assays

    PMID:39044637

    Open questions at the time
    • Whether phenotypes stem from global translation loss versus specific mRNAs unresolved
    • Mitochondrial link mechanism correlative
  16. 2025 High

    Provided the crystal structure of eIF5-CTD bound to eIF2β K-box 3, showing three competitive partner sites and that CK2 phosphomimetics enhance partner affinities, unifying the regulation of exchange and start-codon fidelity.

    Evidence X-ray crystallography, NMR, competition binding, phosphomimetic mutagenesis

    PMID:40670154

    Open questions at the time
    • Structure of 5MP1 and eIF2Bε bound to the same sites not solved
    • In-cell competition dynamics inferred from in vitro affinities
  17. 2025 Medium

    Showed the eIF2β ZBD S264Y mutation relaxes start codon stringency with a distinct sequence-context preference from eIF5 mutants, implying a separable mechanistic role for eIF2β in AUG selection.

    Evidence HIS4-UUG-LacZ context reporters in yeast with β-galactosidase readout

    PMID:41460464

    Open questions at the time
    • Structural basis of context sensitivity not resolved
    • Yeast-only system
  18. 2025 Medium

    Defined a mitochondria–eIF2β axis in neurons where eIF2β upregulation drives autophagic and neuronal defects upon axonal mitochondrial loss.

    Evidence Drosophila genetic gain/loss-of-function epistasis with proteomics and autophagic flux assays

    PMID:41587080

    Open questions at the time
    • Molecular link between eIF2β level and autophagy undefined
    • Mammalian neuronal relevance untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CK2/PP1 phosphocycling, the three competitive K-box partner sites, and the ZBD–γ contact are integrated dynamically in a living cell to switch eIF2β between mRNA recruitment, nucleotide exchange, and fidelity control remains unresolved.
  • No structure of the full eIF2 complex with competing partners bound simultaneously
  • Cellular kinetics of partner exchange unmeasured
  • Mechanism connecting eIF2β to mitochondrial/SMAD4 functions outside canonical initiation undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0045182 translation regulator activity 3 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005730 nucleolus 1 GO:0005829 cytosol 1 GO:0005840 ribosome 1
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-8953854 Metabolism of RNA 2 R-HSA-8953897 Cellular responses to stimuli 2
Partners
CSNK2A1CSNK2BDAP5EIF2B5EIF2S3EIF5PPP1CASMAD4
Complex memberships
43S pre-initiation complexeIF2 heterotrimer

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 The eIF2α subunit is required for structural interactions between eIF2 and eIF2B that promote wild-type rates of nucleotide exchange. Purified eIF2βγ complex (devoid of α-subunit) showed a ~10-fold increase in Km for eIF2B-catalyzed GDP exchange, indicating eIF2α is needed for eIF2B recognition, while Met-tRNAi binding, 43S complex formation, and eIF5-dependent GTP hydrolysis were unaffected by α-subunit absence. Biochemical reconstitution with purified yeast eIF2βγ complex; steady-state kinetic analysis of eIF2B-catalyzed nucleotide exchange; in vitro 43S complex formation and GTP hydrolysis assays The Journal of biological chemistry High 11042214
2003 eIF2β directly binds both the catalytic (CK2α) and regulatory (CK2β) subunits of CK2. The CK2 holoenzyme phosphorylates eIF2β (up to 1.2 mol phosphate/mol), but free CK2α cannot. The N-terminal third of eIF2β contains CK2 phosphorylation sites but is dispensable for CK2 binding; the central/C-terminal region mediates binding to both CK2 subunits. eIF2β inhibits CK2α activity on exogenous substrates (calmodulin, β-casein) but has minor effect on the CK2 holoenzyme. Co-immunoprecipitation in HeLa cells overexpressing HA-tagged eIF2β; direct binding with His6-tagged recombinant proteins; surface plasmon resonance; in vitro phosphorylation assay with truncated/mutant forms The Biochemical journal High 12901717
2002 The archaeal homolog of eIF2β (aIF2β from M. jannaschii) contains two independent structural domains: an N-terminal domain with a four-stranded antiparallel β-sheet and two α-helices (structurally similar to DNA-binding domains), and a C-terminal zinc-binding motif with three antiparallel β-strands coordinated by four conserved cysteines (two CXXC units). These structural features were used to predict the domain architecture of eukaryotic eIF2β. Multidimensional NMR spectroscopy of purified recombinant aIF2β from E. coli Biochemistry High 11980477
2005 The central/C-terminal region of eIF2β (residues 138–333) interacts with CK2α via the basic segment K74–K83 at the beginning of helix αC and residues R191/R195/K198 in the p+1 loop of CK2α. eIF2β-CT stimulates CK2α activity toward a peptide substrate; this stimulation is abolished by the CK2α K74-77A mutation that impairs eIF2β binding. Gel filtration confirmed complex formation. Surface plasmon resonance; truncated/mutant forms of CK2α and eIF2β; in vitro kinase activity assay; gel filtration Molecular and cellular biochemistry Medium 16335529
2006 CK2 directly phosphorylates eIF2β at Ser2 (main constitutive site) and Ser67 in living HeLa cells. The N-terminal region of eIF2β is required for its full function: overexpression of N-terminally truncated eIF2β (eIF2β-CT) causes cell death and fails to bind eIF5, while the eIF2β S2/67A mutant slows serum-stimulated protein synthesis. The S2/67A mutant does not affect incorporation into the eIF2 trimer or binding to eIF5 and CK2α. CK2 chemical inhibitors (emodin, apigenin); transfection of kinase-dead CK2α K68A; phosphorylation-site mutants (S2A, S67A, S2/67A) and truncated forms; reporter assays for protein synthesis; co-immunoprecipitation for complex assembly The Biochemical journal High 16225457
2006 eIF2β physically interacts with protein phosphatase 1 (PP1) via an RVxF motif in its central region and at least one additional C-terminal binding site. eIF2β acts as an inhibitor of PP1-mediated dephosphorylation of glycogen phosphorylase and eIF2α-Ser51 but activates its own dephosphorylation at Ser2, Ser67, and Ser218 by associated PP1; mutation of the RVxF motif reduces eIF2β's substrate quality for PP1. Overexpression of WT vs. RVxF-mutant eIF2β did not differentially affect basal translation rates. PP1-binding assay; co-immunoprecipitation from cell lysates; pull-down with purified components; site-directed mutagenesis of RVxF motif; in vitro phosphatase activity assays The Biochemical journal High 16987104
2007 The eIF2Bε GEF domain makes distinct contacts with eIF2β and eIF2γ to catalyze nucleotide exchange. Conserved residue W699 of eIF2Bε is critical for interaction with eIF2β, whereas L568 and E569 (near the universally conserved E569) are critical for interaction with eIF2γ but not for eIF2β binding. E569D substitution is lethal; W699 mutation abolishes eIF2β binding. Multiple contacts between eIF2γ and eIF2Bε are necessary for exchange activity. Site-directed mutagenesis of conserved eIF2Bε surface residues; genetic complementation (lethality tests in yeast); binding assays between eIF2Bε mutants and eIF2 subunits; GCN4 reporter assay for GEF activity Molecular and cellular biology High 17526738
2012 The CTD of eIF5 binds eIF2β via overlapping surfaces with eIF1 on eIF5-CTD, as determined by NMR. Mutations in eIF5-CTD that disrupt binding to both eIF1 and eIF2β impair start codon recognition and prevent eIF1 release from the PIC, demonstrating that eIF5-CTD switches PICs from an open to a closed state through its dynamic interplay with eIF2β. NMR spectroscopy to map binding sites; site-directed mutagenesis of eIF5-CTD; genetic complementation in yeast; biochemical PIC assembly assays Cell reports High 22813744
2012 The eIF2β K-boxes (Lys-rich repeats) promote mRNA binding to the 40S subunit in vitro; this activity is reversed by eIF5-CTD. Mutations altering eIF4G-RS1, eIF2β K-boxes, and eIF5-CTD restore start codon selection accuracy, indicating that sequential binding of eIF5 to eIF4G and eIF2β within the PIC primes the ribosome for AUG recognition and assists eIF1 release. In vitro mRNA binding to 40S assays with purified factors; genetic epistasis in yeast; GCN4 reporter assay for start codon fidelity; protein-protein interaction assays Molecular and cellular biology High 22851688
2012 In yeast eIF2, the eIF2β β-subunit (particularly its eukaryote-specific N- and C-terminal domains) makes the dominant contribution to Met-tRNAi binding affinity in the context of chimeric eIF2 complexes (yeast α/β + archaeal γ). The eIF2α subunit has a modest contribution that can be increased by shortening the acidic C-terminal extension of α. Purification of chimeric eIF2 complexes; tRNA binding assays; small-angle X-ray scattering (SAXS) Nucleic acids research High 23193270
2015 DAP5 (an eIF4G homolog) physically associates with eIF2β and eIF4AI to stimulate IRES-dependent translation of cellular mRNAs. DAP5 is dispensable for cap-dependent translation, making eIF2β part of a selective cap-independent translation complex. Co-immunoprecipitation; IRES reporter assays; DAP5 knockdown/depletion with rescue experiments Nucleic acids research Medium 25779044
2016 A specific mutation in eIF2β prevents eIF5 from acting as a GDP-dissociation inhibitor (GDI) on eIF2•GDP, altering cellular responses to reduced eIF2B GEF activity and impairing GCN4 translational induction under amino acid starvation. The eIF2β mutation does not affect eIF2's intrinsic affinity for guanine nucleotides, Met-tRNAi, or 43S PIC components; instead it prevents eIF5 GDI from stabilizing GDP binding to eIF2γ, thereby increasing the GDP off-rate from eIF2•GDP/eIF5 complexes. Fluorescent nucleotide binding assays with purified eIF2; initiator tRNA binding assays; eIF5 GDI assay; genetic growth assays; GCN4 reporter assay Nucleic acids research High 27458202
2017 Deletion of the polylysine K-box stretches in eIF2β (eIF2βΔ3K) creates a dominant-negative that reduces protein synthesis, causes G2 cell cycle arrest, and increases cell death in HEK293 cells. The polylysine stretches are required for translocation of eIF2β from the cytoplasm to the nucleus/nucleolus; eIF2βΔ3K fails to translocate. Tetracycline-inducible expression of eIF2βΔ3K in HEK293 TetR cells; gene reporter assay for translation; western blot; flow cytometry; cell proliferation assay; confocal immunofluorescence for subcellular localization Cancer biology & therapy Medium 28692326
2024 The zinc-binding domain (ZBD) of eIF2β interacts with eIF2γ via the guanine nucleotide-binding interface (a second binding site beyond the previously known α1-helix contact) to promote Met-tRNAi binding. The eIF2βS264Y ZBD mutation causes eIF2β–γ interaction defect and Met-tRNAi binding defect; the intragenic suppressor eIF2βT238A restores both interactions. eIF2β ZBD residues Asn252Asp and Arg253Ala mutations also cause Met-tRNAi binding defects partially rescued by T238A. In vivo yeast genetics (suppressor mutation analysis); in vitro eIF2 subunit binding assays; Met-tRNAi binding assays; GTPase activity measurement Bioscience reports Medium 38873976
2025 X-ray crystal structure of yeast eIF5-CTD in complex with eIF2β K-box 3 reveals an extended binding site on eIF2β extending far beyond the K-box. eIF2β contains three distinct binding sites (centered on each K-box), and human eIF5, eIF2Bε, and 5MP1 can each bind all three sites with mutually reduced affinities. CK2 phosphomimetic mutations on eIF2β increase affinities for eIF5, eIF2Bε, and 5MP1. eIF2B accelerates eIF5 dissociation from eIF2-GDP to promote nucleotide exchange; 5MP1 destabilizes eIF5 binding to eIF2 and the PIC to promote stringent start codon selection. X-ray crystallography (crystal structure of eIF5-CTD/eIF2β K-box 3 complex); NMR spectroscopy; binding affinity measurements; phosphomimetic mutagenesis RNA (New York, N.Y.) High 40670154
2024 Premeiotic deletion of Eif2s2 in mice causes oocyte arrest at the pachytene/early diplotene stage followed by apoptosis and failure of primordial follicle formation. Mechanistically, Eif2s2 deletion downregulates homologous recombination-related and mitochondrial fission-related proteins, upregulates integrated stress response proteins, suppresses dictyate gene expression, and impairs mitochondrial function (elongated morphology, decreased ATP, mtDNA copy number, ROS accumulation). DNA damage response and pro-apoptotic proteins increase while anti-apoptotic proteins decrease. Conditional knockout (premeiotic germ cell-specific Eif2s2 deletion); western blot for protein levels; immunofluorescence; mitochondrial function assays (ATP, ROS, mtDNA); TUNEL/cleaved-Caspase-3 for apoptosis; Lamin B1 staining Cell proliferation Medium 39044637
2009 Partial deficiency of Eif2s2 (eIF2β) reduces testicular germ cell tumor (TGCT) incidence ~2-fold in mice and attenuates germ cell proliferation and differentiation. Complete deficiency of Eif2s2 causes embryonic lethality near implantation, establishing that eIF2β is essential for early development and that TGCT pathogenesis is sensitive to eIF2 complex availability. Mouse genetics: heterozygous Eif2s2 deletion analysis; comparison with Raly gene-trap and agouti transgenic/viable-yellow mutants for TGCT incidence; analysis of embryonic lethality timing Human molecular genetics Medium 19168544
2025 In Drosophila neurons, eIF2β is upregulated upon depletion of axonal mitochondria. Neuronal overexpression of eIF2β phenocopies autophagic defects and neuronal dysfunction caused by axonal mitochondria depletion. Lowering eIF2β expression rescues the autophagic defects and neuronal dysfunctions caused by axonal mitochondria depletion. eIF2α phosphorylation is reduced by axonal mitochondria depletion, with global translation suppression. Drosophila genetic manipulation (axonal mitochondria depletion, eIF2β overexpression and knockdown); proteome analysis; autophagic flux assays; neuronal function assays; western blot for eIF2α phosphorylation eLife Medium 41587080
2024 eIF2S2 physically interacts with SMAD4 via its N-terminus binding to the MH-1 domain of SMAD4, as shown by co-immunoprecipitation and BiFC assay. eIF2S2 knockdown increases SMAD4 protein levels without changing SMAD4 mRNA, indicating post-translational regulation of SMAD4 by eIF2S2. eIF2S2 overexpression reduces SMAD4 levels and weakens promoter activity of SMAD4-regulated antiproliferative genes p15 and p27 in cervical cancer cells. Co-immunoprecipitation; bimolecular fluorescence complementation (BiFC); siRNA knockdown; transient overexpression; qRT-PCR for mRNA; luciferase promoter assay Biomolecules & therapeutics Medium 39370734
2025 In yeast, the eIF2βS264Y mutation (in the ZBD) causes a Sui- (suppressor of initiation codon) phenotype, initiating translation at near-cognate UUG codons in addition to AUG. UUG start codon recognition by eIF2βS264Y is strongly influenced by surrounding nucleotide context, with purines at -3 and -1 positions favoring aberrant UUG initiation. eIF2βS264Y shows distinct context preferences from eIF5G31R, implying distinct mechanistic roles. HIS4-UUG-LacZ reporter constructs with varied -3 to -1 nucleotide contexts transformed into yeast carrying eIF2βS264Y; β-galactosidase activity assay Biochemical genetics Medium 41460464

Source papers

Stage 0 corpus · 27 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 DAP5 associates with eIF2β and eIF4AI to promote Internal Ribosome Entry Site driven translation. Nucleic acids research 79 25779044
2012 The C-terminal domain of eukaryotic initiation factor 5 promotes start codon recognition by its dynamic interplay with eIF1 and eIF2β. Cell reports 65 22813744
2001 Biochemical analysis of the eIF2beta gamma complex reveals a structural function for eIF2alpha in catalyzed nucleotide exchange. The Journal of biological chemistry 50 11042214
2020 RBP EIF2S2 Promotes Tumorigenesis and Progression by Regulating MYC-Mediated Inhibition via FHIT-Related Enhancers. Molecular therapy : the journal of the American Society of Gene Therapy 39 32059763
2009 Deletion of eIF2beta suppresses testicular cancer incidence and causes recessive lethality in agouti-yellow mice. Human molecular genetics 38 19168544
2012 Sequential eukaryotic translation initiation factor 5 (eIF5) binding to the charged disordered segments of eIF4G and eIF2β stabilizes the 48S preinitiation complex and promotes its shift to the initiation mode. Molecular and cellular biology 31 22851688
2007 Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange. Molecular and cellular biology 28 17526738
2003 Eukaryotic translation-initiation factor eIF2beta binds to protein kinase CK2: effects on CK2alpha activity. The Biochemical journal 28 12901717
2018 eIF2β, a subunit of translation-initiation factor EIF2, is a potential therapeutic target for non-small cell lung cancer. Cancer science 23 29624814
2006 The N-terminal domain of the human eIF2beta subunit and the CK2 phosphorylation sites are required for its function. The Biochemical journal 23 16225457
2016 eIF2β is critical for eIF5-mediated GDP-dissociation inhibitor activity and translational control. Nucleic acids research 21 27458202
2006 The translation initiation factor eIF2beta is an interactor of protein phosphatase-1. The Biochemical journal 18 16987104
2002 Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins. Biochemistry 18 11980477
2012 Roles of yeast eIF2α and eIF2β subunits in the binding of the initiator methionyl-tRNA. Nucleic acids research 16 23193270
2021 18F-FDG PET/CT metabolic parameters correlate with EIF2S2 expression status in colorectal cancer. Journal of Cancer 15 34475997
2016 Identification of Plasmodium falciparum Translation Initiation eIF2β Subunit: Direct Interaction with Protein Phosphatase Type 1. Frontiers in microbiology 12 27303372
2024 Premeiotic deletion of Eif2s2 causes oocyte arrest at the early diplotene stage and apoptosis in mice. Cell proliferation 7 39044637
2017 Deletion of eIF2β lysine stretches creates a dominant negative that affects the translation and proliferation in human cell line: A tool for arresting the cell growth. Cancer biology & therapy 7 28692326
2005 Cross talk between protein kinase CK2 and eukaryotic translation initiation factor eIF2beta subunit. Molecular and cellular biochemistry 5 16335529
2024 EIF2S2 transcriptionally upregulates HIF1α to promote gastric cancer progression via activating PI3K/AKT/mTOR pathway. Carcinogenesis 3 39046731
2025 Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2. RNA (New York, N.Y.) 2 40670154
2026 Axonal distribution of mitochondria maintains neuronal autophagy during aging via eIF2β. eLife 1 41587080
2025 Axonal distribution of mitochondria maintains neuronal autophagy during aging via eIF2β. bioRxiv : the preprint server for biology 1 38293064
2024 Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2. bioRxiv : the preprint server for biology 1 38712236
2024 eIF2β zinc-binding domain interacts with the eIF2γ subunit through the guanine nucleotide binding interface to promote Met-tRNAiMet binding. Bioscience reports 1 38873976
2025 Translation Initiation Fidelity Defective Mutations in eIF5 and eIF2β Show Distinct Sensitivity to the Sequence Context for Recognition of the UUG Start Codon. Biochemical genetics 0 41460464
2024 Translation Initiation Factor-2S2 (eIF2S2) Contributes to Cervical Carcinogenesis by Inhibiting the TGF-β/SMAD4 Signaling Pathway. Biomolecules & therapeutics 0 39370734

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