| 1998 |
TRIP-1 (EIF3I) associates with the TGF-β type II receptor and is phosphorylated by it. TRIP-1 overexpression represses TGF-β-induced transcription from the PAI-1 promoter and inhibits PAI-1 expression induced by Smads and activated TGF-β type I receptors, acting through both receptor-dependent and receptor-independent mechanisms. Deletion mutational analysis identified two distinct non-WD40 regions required for this inhibitory activity. |
Co-IP/association assay, reporter gene assay (PAI-1 promoter), deletion mutagenesis, transfection overexpression |
The Journal of biological chemistry |
Medium |
9813058
|
| 2010 |
A single-point mutation in WD40 repeat 6 of yeast eIF3i/Tif34 (Q258R) causes severe growth defects, decreases the rate of translation initiation in vivo, diminishes GCN4 induction, and impairs the rate of scanning of post-termination 40S ribosomes moving downstream from uORF1, without affecting eIF3 complex integrity or 43S PIC formation. This implicates eIF3i in stimulation of linear scanning. |
Genetic point mutation, in vivo translation assays, GCN4 reporter assay, polysome analysis |
Molecular and cellular biology |
High |
20679478
|
| 2006 |
Overexpression of eIF3i in human cells causes cell size increase, proliferation enhancement, cell-cycle progression, and anchorage-independent growth in an mTOR-dependent manner; rapamycin (mTOR inhibitor) reduces serine phosphorylation of eIF3i and abolishes anchorage-independent growth, indicating mTOR phosphorylates eIF3i on serine and that this is required for its oncogenic activity. |
Overexpression in cell lines, rapamycin treatment, phosphorylation assay, anchorage-independent growth assay |
Molecular carcinogenesis |
Medium |
16929481
|
| 2013 |
eIF3I physically interacts with Akt1 in HCC cell lines and tissues; the C-terminal domain of eIF3I interacts with the Akt1 kinase domain. This interaction prevents PP2A-mediated dephosphorylation of Akt1, resulting in constitutively active Akt1 oncogenic signaling. Dominant negative Akt1 or antisense eIF3I suppresses eIF3I-mediated tumorigenesis. |
Co-IP in cell lines and tissues, oncogenic domain mapping, dominant-negative mutant rescue, in vitro and in vivo tumorigenesis assays, PP2A dephosphorylation assay |
Hepatology (Baltimore, Md.) |
High |
23460382
|
| 2013 |
eIF3i overexpression in intestinal epithelial cells directly upregulates COX-2 protein synthesis at the translational level and activates the β-catenin/TCF4 signaling pathway, driving colon oncogenesis. |
Ectopic overexpression, polysome profiling/translational assay, reporter assays for β-catenin/TCF4, in vitro oncogenesis assays |
Oncogene |
Medium |
24056964
|
| 2014 |
eIF3i is required for VEGFA protein expression under hypoxia. HIF1A binds the eIF3i promoter and activates eIF3i transcription under hypoxia. eIF3i knockdown specifically reduces translational efficiency of VEGFA mRNA without causing general translation repression, establishing eIF3i as a selective translational regulator of VEGFA downstream of HIF1A. |
ChIP for HIF1A at eIF3i promoter, siRNA knockdown, polysome profiling, zebrafish eIF3i mutant angiogenesis assay, tumor xenograft angiogenesis model |
The Journal of biological chemistry |
High |
25147179
|
| 2014 |
In primary human lung fibroblasts, knockdown of TRIP-1 (EIF3I) drives fibroblast-to-myofibroblast transdifferentiation (α-SMA induction, collagen contraction, apoptosis resistance) via enhanced AKT phosphorylation, independent of Smad3 signaling. A constitutively active AKT construct mimics TRIP-1 knockdown effects, and AKT inhibition prevents α-SMA induction in TRIP-1 knockdown cells. |
siRNA knockdown, plasmid overexpression, AKT inhibitor treatment, constitutively active AKT construct, α-SMA expression assay, collagen contraction assay, Smad3 knockdown epistasis |
Respiratory research |
Medium |
24528651
|
| 2015 |
CLU (clusterin) activates Akt signaling by complexing with EIF3I; this complex promotes MMP13 expression and HCC metastasis. CLU knockdown via OGX-011 suppresses HCC metastasis through inhibiting EIF3I/Akt/MMP13 signaling. |
Co-IP (CLU-EIF3I complex), in vitro and in vivo invasion/metastasis assays, CLU knockdown, pathway inhibition |
Oncotarget |
Medium |
25609201
|
| 2017 |
eIF3i knockdown in endothelial cells reduces VEGFR2 and ERK protein expression (selective translational downregulation), restraining endothelial cell proliferation and migration. In zebrafish, eIF3i mutant endothelial cells fail to respond to tumor-derived induction signals, establishing eIF3i as a selective translational regulator of VEGFR/ERK signaling in endothelial cells. |
siRNA knockdown, zebrafish eIF3i mutant, cell proliferation/migration assays, Western blot for VEGFR2/ERK, gene therapy shRNA model |
Oncotarget |
Medium |
28193911
|
| 2017 |
EIF3I physically interacts with VSV matrix protein (M protein) as identified by yeast two-hybrid, validated by GST pull-down and co-localization. Mutagenesis of M (aa 122–181) impairs but does not abolish the interaction. EIF3I knockdown modulates VSV replication/transcription in a time-dependent manner and inhibits ISG expression regulated by phospho-Akt1. |
Yeast two-hybrid, GST pull-down, laser confocal co-localization, mutagenesis of M protein, siRNA knockdown, viral replication assay |
Veterinary microbiology |
Medium |
29173589
|
| 2018 |
TRIP-1 (EIF3I) is localized in the extracellular matrix of bone and dentin, and promotes nucleation of calcium phosphate polymorphs including hydroxyapatite crystals. Recombinant TRIP-1 at varying concentrations orchestrates hydroxyapatite formation on demineralized dentin collagen under physiological conditions. |
In vivo implantation assay, recombinant protein nucleation experiments, TEM analysis of mineral deposits, overexpression/knockdown ECM analysis |
Connective tissue research |
Medium |
29745814
|
| 2021 |
PD-L1 directly binds EIF3I and promotes cutaneous wound healing by downregulating IRS4; the EIF3I–PD-L1–IRS4 axis was identified by immunoprecipitation combined with mass spectrometry and validated by co-immunoprecipitation assays with in vivo and in vitro functional testing. |
Co-IP with mass spectrometry, co-immunoprecipitation validation, in vivo and in vitro functional assays for wound healing |
The Journal of investigative dermatology |
Medium |
34293353
|
| 2022 |
Lenalidomide (via the E3 ligase adapter CRBN) recruits eIF3i but does not degrade it; instead, it sequesters eIF3i from the eIF3 complex. The binding interface on eIF3i was identified by a covalent lenalidomide probe and mass spectrometry. This sequestration drives effects on angiogenic markers, Akt1 phosphorylation, and antiangiogenesis phenotypes. |
Covalent chemical probe + mass spectrometry mapping of binding interface, chemical proteomics, Co-IP for eIF3 complex disruption, cell-based angiogenesis and Akt1 phosphorylation assays |
ACS chemical biology |
High |
36325969
|
| 2023 |
eIF3i directly promotes PHGDH translation in colorectal cancer cells. METTL3-mediated m6A modification on PHGDH mRNA promotes its binding to eIF3i, leading to higher translational rate of PHGDH. PHGDH knockdown partially attenuates the excessive growth induced by eIF3i overexpression. |
Ribosome profiling, proteomics, m6A modification analysis, RIP assay for eIF3i-PHGDH mRNA binding, siRNA knockdown epistasis, in vivo tumor growth assay |
The Journal of biological chemistry |
High |
37611825
|
| 2024 |
lnc-TSPAN12 acts as a scaffold that enhances the SENP1-EIF3I interaction, inhibiting SUMOylation of EIF3I and preventing its ubiquitin-mediated degradation, thereby stabilizing EIF3I protein levels and activating Wnt/β-catenin signaling to promote EMT and HCC metastasis. |
Co-IP (EIF3I-SENP1 interaction), RNA pull-down, SUMOylation assay, ubiquitination assay, lncRNA knockdown/overexpression, in vivo metastasis assay |
Oncogene |
Medium |
38374407
|
| 2025 |
eIF3i directly binds NELFCD mRNA and promotes its translation, independent of transcription. eIF3i-driven NELFCD upregulation facilitates EMT and invadopodia formation, promoting CRC metastasis. NELFCD knockdown abolishes the pro-metastatic effects of eIF3i overexpression. |
Polysome profiling, RNA-binding assays (RIP and RNA pull-down), in vitro migration/invasion assays, in vivo mouse metastatic models, epistasis knockdown |
British journal of cancer |
Medium |
41315067
|
| 2025 |
Loss-of-function mutations in eIF3i (yeast ortholog) reduce translation of GFP reporters with both short and long unstructured 5′ UTRs to a similar extent as mutations in other scanning factors (eIF4A, Ded1, eIF4G, eIF4B, eIF3g), and severely diminish translation of reporters with structured 5′ UTRs. This is consistent with eIF3i facilitating mRNA scanning and secondary structure unwinding rather than being the rate-limiting helicase-driven translocase. |
GFP reporter assay in S. cerevisiae, loss-of-function mutations in eIF3i and comparison with other initiation factor mutants |
bioRxivpreprint |
Low |
bio_10.1101_2024.12.30.630811
|