| 2009 |
CTIF contains a MIF4G domain and directly interacts with CBP80 (nuclear cap-binding protein 80), forming part of the CBP80/20-dependent translation initiation complex. Depletion of endogenous CTIF from an in vitro translation system selectively blocks translation of CBP80-bound mRNAs, while addition of purified CTIF restores it. CTIF localizes to the perinuclear region by confocal microscopy. Down-regulation of CTIF also abrogates nonsense-mediated mRNA decay (NMD). |
In vitro translation reconstitution with recombinant protein add-back, co-immunoprecipitation (Co-IP), siRNA knockdown, confocal microscopy |
Genes & development |
High |
19648179
|
| 2012 |
CTIF specifically interacts with eIF3g (a component of the eIF3 ribosome-recruitment complex) and serves as an adaptor protein bridging CBP80/20 to eIF3 during CBC-dependent translation. Down-regulation of CTIF redistributes CBP80 from polysome fractions to subpolysome fractions without affecting eIF4E distribution. Artificial tethering of CTIF to an intercistronic region of dicistronic mRNA drives downstream cistron translation in an eIF3-dependent manner. |
Co-immunoprecipitation, siRNA knockdown with polysome fractionation, tethering assay with dicistronic reporter |
The Journal of biological chemistry |
High |
22493286
|
| 2012 |
CTIF interacts with stem-loop binding protein (SLBP) — identified via yeast two-hybrid screening — and SLBP preferentially associates with the CBC-dependent translation (CT) complex of histone mRNAs. Rapid degradation of histone mRNA upon inhibition of DNA replication largely occurs on CBP80/20-bound (CT) mRNAs rather than eIF4E-bound mRNAs. |
Yeast two-hybrid screening, co-immunoprecipitation, polysome fractionation, mRNA stability assays |
Nucleic acids research |
Medium |
23234701
|
| 2013 |
The MIF4G domain of CTIF is structurally related to SLIP1 and shares conserved SBM (SLIP1-binding motif)-binding and homodimerization residues, suggesting CTIF can form a SLIP1-CTIF heterodimer as a platform to bridge SLBP with translation initiation factors. |
Crystal structure of SLIP1-SLBP (2.5 Å) and SLIP1-DBP5 (3.25 Å), pull-down assays, sequence conservation analysis |
Nucleic acids research |
Medium |
23804756
|
| 2014 |
eIF4AIII (an EJC component) is recruited to the 5'-end of CBC-bound mRNAs through direct interaction with CTIF, independently of deposited EJCs. This recruitment promotes unwinding of 5'UTR secondary structures and enhances CBC-dependent translation both in vivo and in vitro. |
Co-immunoprecipitation, in vitro reconstitution with recombinant proteins, polysome fractionation, tethering assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
25313076
|
| 2014 |
CTIF interacts with SLBP and this interaction is important for efficient histone mRNA translation. Upon inhibition of DNA replication or at the end of S phase, hyperphosphorylated UPF1 (phosphorylated by ATR and DNA-PK) competes with CTIF for SLBP binding, displacing CTIF and eIF3 from the SLBP-containing histone mRNP, thereby switching histone mRNA from translation to degradation mode. |
Co-immunoprecipitation, competition binding assay, siRNA knockdown, kinase inhibitor treatment |
Nucleic acids research |
Medium |
25016523
|
| 2017 |
CTIF forms a trimeric CED complex with eEF1A1 and DCTN1 (dynactin subunit 1) that selectively recognizes misfolded polypeptides and targets them to the aggresome via retrograde transport. When UPS is impaired, CTIF is sequestered into the aggresome, which reduces CBC-dependent translation and renders cells more resistant to proteotoxic-stress-induced apoptosis. |
Co-immunoprecipitation, live-cell imaging, siRNA knockdown, aggresome formation assay, apoptosis assay |
Nature communications |
High |
28589942
|
| 2017 |
The CED complex (CTIF-eEF1A1-DCTN1) functions as aggresome-targeting machinery; CTIF release from the CT (CBC-dependent translation) complex accompanies aggresomal targeting, establishing crosstalk between translational inhibition and aggresome formation under proteotoxic stress. |
Co-immunoprecipitation, imaging of aggresome formation, translation assays (review/commentary with direct reference to experimental findings of PMID:28589942) |
Autophagy |
Medium |
28837386
|
| 2018 |
CTIF is a novel PARylation target of tankyrase enzymes at the centrosomal region, identified by a genome-wide PAR-biosensor screen. CTIF plays a role in the distribution of centrosomal satellites. |
Bimolecular fluorescent complementation PAR biosensor, transposon-mediated genome-wide screen, live-cell imaging |
Nature communications |
Medium |
29789535
|
| 2020 |
Hyperphosphorylated UPF1 promotes aggresome formation by interacting with the CTIF-eEF1A1-DCTN1 (CED) complex. Single-particle visualization shows UPF1 increases both the frequency and fidelity of movement of CTIF aggregates toward the aggresome. UPF1 hyperphosphorylation suppresses proteotoxic-stress-induced apoptosis. |
Co-immunoprecipitation, single-particle live-cell imaging, siRNA knockdown, phosphomimetic mutant analysis, apoptosis assay |
Nature communications |
High |
32561765
|
| 2020 |
CTIF inhibits HIV-1 and HIV-2 Gag synthesis from the full-length viral RNA. CTIF associates with HIV-1 Rev through its N-terminal domain and is recruited onto the full-length RNA ribonucleoprotein complex, where it interferes with Gag synthesis. CTIF also induces cytoplasmic accumulation of Rev, impeding Rev's association with CBP80. Conversely, Rev competes with CTIF for CBP80 binding. |
Co-immunoprecipitation, siRNA knockdown, reporter assays, subcellular fractionation |
RNA biology |
Medium |
33103564
|
| 2021 |
TRIM28 directly interacts with CTIF and acts as a negative regulator of aggresome formation: the TRIM28-CTIF interaction leads to inefficient aggresomal targeting of misfolded polypeptides. Viral infection (influenza A) or poly I:C treatment triggers phosphorylation of TRIM28 at S473 by double-stranded RNA-activated protein kinase (PKR/EIF2AK2), which promotes TRIM28-CTIF association, inhibits aggresome formation, and suppresses viral proliferation. |
Co-immunoprecipitation, proximity ligation assay (PLA), siRNA knockdown, phosphomimetic mutants, aggresome formation assay, viral proliferation assay |
Autophagy |
High |
33783327
|
| 2021 |
CTIF is tethered in a translationally incompetent state to the perinuclear region by the DEAD-box helicase DDX19B. Upon mRNA export, DDX19B hands CTIF over to CBP80 associated with the 5'-cap of newly exported mRNA, forming the CBP80-CTIF complex that initiates CBC-dependent translation at the perinuclear region. Disrupting the CTIF-DDX19B interaction leads to uncontrolled CBC-dependent translation throughout the cytosol and dysregulates NMD. |
Co-immunoprecipitation, siRNA knockdown, reporter assays, confocal microscopy, polysome fractionation |
Nucleic acids research |
High |
34232997
|
| 2023 |
YTHDF2 is recruited to the misfolded polypeptide-associated complex containing UPF1, CTIF, eEF1A1, and DCTN1 through its interaction with UPF1 (m6A-independent). YTHDF2 increases the interaction between dynein motor protein and the misfolded polypeptide-associated complex, facilitating movement of misfolded polypeptides toward aggresomes. |
Co-immunoprecipitation, siRNA knockdown, live-cell imaging of aggresome dynamics, apoptosis assay |
Nature communications |
Medium |
37803021
|