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Eukaryotic translation initiation factor 3, subunit G

eIF3g, TIF35, eIF3-p44, Tif35p, eIF3-p33
Top mentioned proteins: PRT1, CAN, 110-kDa, V1a, eIF3j
Papers on eIF3g
Control of Paip1-eukayrotic translation initiation factor 3 interaction by amino acids through S6 kinase.
Sonenberg et al., Montréal, Canada. In Mol Cell Biol, 2014
We previously showed that the interaction of PABP-interacting protein 1 (Paip1) with PABP and eukaryotic translation initiation factor 3 (eIF3; via the eIF3g subunit) further stimulates translation.
Evidence for the role of wheat eukaryotic translation initiation factor 3 subunit g (TaeIF3g) in abiotic stress tolerance.
Singh et al., Amritsar, India. In Gene, 2014
The gene encoding eIF3g (TaeIF3g), one of the 11 subunits of eukaryotic translation initiation factor 3 (eIF3), was cloned from wheat for carrying out its functional analysis.
Caspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g).
Lee et al., Taejŏn, South Korea. In Febs Lett, 2013
In this study, we found that the activation of caspases by cisplatin in T24 cells induces the cleavage of subunit G of the eIF3 complex (eIF3g).
Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex.
Zhang et al., Indianapolis, United States. In J Biol Chem, 2013
A subcomplex consisting of eIF3a, eIF3b, eIF3g, and eIF3i (eIF3(a:b:i:g)) has also been identified.
Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.
Conti et al., Chapel Hill, United States. In Nucleic Acids Res, 2013
We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5.
Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g.
GeneRIF
Kim et al., Seoul, South Korea. In J Biol Chem, 2012
down-regulation of eIF3g inhibits the efficiency of nonsense-mediated mRNA decay, which is tightly coupled to CT but not to ET
Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly.
Valásek et al., Praha, Czech Republic. In Nucleic Acids Res, 2012
Mutating these interactions displays severe growth defects and eliminates association of eIF3i/TIF34 and strikingly also eIF3g/TIF35 with eIF3 and 40S subunits in vivo.
Assessing the components of the eIF3 complex and their phosphorylation status.
Link et al., Nashville, United States. In J Proteome Res, 2011
The yeast eIF3 complex contains five core components: Rpg1, Nip1, Prt1, Tif34, and Tif35.
Quantitative profiling of in vivo-assembled RNA-protein complexes using a novel integrated proteomic approach.
Waterman et al., Irvine, United States. In Mol Cell Proteomics, 2011
With a conventionally translated target RNA as control, 36 IRES binding proteins have been quantitatively identified including known IRES binding factors, novel interacting proteins, translation initiation factors (eIF4A-1, eIF-2A, and eIF3g), and ribosomal subunits with known noncanonical actions (RPS19, RPS7, and RPL26).
[Construction and application of inducible artificial microRNA expression vector targeting eIF3g gene].
Cao et al., Hangzhou, China. In Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi, 2011
AIM: To construct an inducible artificial microRNA expression vector targeting eIF3g gene and use it to inhibit the expression of eIF3g in K562 cells.
The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning.
GeneRIF
Valásek et al., Praha, Czech Republic. In Mol Cell Biol, 2010
Data show that mutations of eIF3 subunits, g/Tif35 and i/Tif34 diminish induction of GCN4 expression.
Pelota interacts with HAX1, EIF3G and SRPX and the resulting protein complexes are associated with the actin cytoskeleton.
GeneRIF
Adham et al., Göttingen, Germany. In Bmc Cell Biol, 2009
PELO is subcellularly localized at the actin cytoskeleton, interacts with HAX1, EIF3G and SRPX proteins and that this interaction occurs at the cytoskeleton; this interaction may facilitate PELO to detect and degrade aberrant mRNAs.
Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation.
Sonenberg et al., Montréal, Canada. In Mol Cell Biol, 2008
Here, we describe the interaction between Paip1 and eIF3, which is direct, RNA independent, and mediated via the eIF3g (p44) subunit.
Fission yeast translation initiation factor 3 subunit eIF3h is not essential for global translation initiation, but deletion of eif3h+ affects spore formation.
Maitra et al., New York City, United States. In Yeast, 2008
We show that this protein physically associates with the 40S ribosomal particles as a constituent of the multimeric eIF3 protein complex, which consists of all five known eIF3 core subunits (eIF3a, eIF3b, eIF3c, eIF3g and eIF3i) as well as the five non-core subunits (eIF3d, eIF3e, eIF3f, eIF3h and eIF3m) that constitute an eIF3 holocomplex in fission yeast.
Gene expression profiling related to the enhanced erythropoiesis in mouse bone marrow cells.
Lee et al., Kwangju, South Korea. In J Cell Biochem, 2008
Among the six candidates, eIF3-p44, hnRNPH1, G3bp, and Zfpm-1 were dramatically increased at day 7 of the in vitro erythropoietic differentiation of human CD34(+) cells.
Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g).
GeneRIF
Lim et al., Seoul, South Korea. In Febs Lett, 2006
AIF overexpression specifically resulted in the activation of caspase-7, thereby amplifying the inhibition of protein
A functional link between Disrupted-In-Schizophrenia 1 and the eukaryotic translation initiation factor 3.
GeneRIF
Akiyama et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2006
Furthermore, we found that overexpression of DISC1 in SH-SY5Y cells induces the assembly of eIF3- and TIA-1-positive stress granules (SGs), discrete cytoplasmic granules formed in response to environmental stresses.
A plant viral "reinitiation" factor interacts with the host translational machinery.
Impact
Ryabova et al., Basel, Switzerland. In Cell, 2001
Two proteins mediating these interactions were identified: eIF3g and 60S ribosomal protein L24.
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