Publication for EIF3E and EIF3D

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	EIF3E	eukaryotic translation initiation factor 3 subunit E	3646			[link]
hsa	EIF3D	eukaryotic translation initiation factor 3 subunit D	8664

Pubmed ID	Priority	Text
29747599	0.98	EIF3D, EIF3E, EIF3F, EIF3H) genes.
27477275	0.97	eIF3d-eIF3e module of eIF3 in a translational circuit to uphold metabolic balance that may be disrupted in human cancer.
	0.97	eIF3d and eIF3e.
	0.97	eIF3d and eIF3e together serve as specificity module to drive the synthesis of mitochondrial proteins.
	0.97	eIF3d-eIF3e module regulate specific mRNAs?
	0.97	eIF3d and eIF3e directs the synthesis of mitochondrial ETC components and other mitochondrial proteins leading to efficient respiration and ATP production (left panel).
	0.96	eIF3d and suggests that eIF3d and eIF3e are recruited into the complex as a module.
	0.93	eif3d and eif3e causes respiratory deficiency and oxidative stress, a compensatory upregulation of glycolysis, strong dependence on glucose, and reduced lifespan (Fig. 7).
	0.93	eIF3d-eIF3e dimer.
	0.91	eIF3d-eIF3e as a specificity module
	0.91	eIF3e and eIF3d are not globally defective in protein synthesis as they are translating the compensatory response mRNAs encoding glycolytic enzymes and the glucose transporter Ght5p with greater efficiency than wild-type cells.
	0.90	eIF3d-eIF3e module in cellular physiology and aging.
	0.89	eif3e and eif3d are dependent on glucose
	0.83	eIF3d is stably associated with 80S complexes in cells deleted for eif3e (Fig. S1B).
	0.83	eif3e and eif3d deleted cells under limiting glucose conditions.
	0.77	eif3e and eif3d deleted cells
	0.73	eIF3e and eIF3d causes endogenous oxidative stress and premature aging
	0.62	eIF3e and eIF3d were entirely unable to grow in media containing non-fermentable glycerol as the carbon source (Fig. 4D), confirming that they are severely impaired in respiration.
	0.62	eif3e and eif3d on protein synthesis
27210288	0.97	eIF3d (brown), eIF3e (green), eIF3f (cyan), eIF3h (yellow), eIF3k (magenta), eIF3l (orange), and eIF3m (light pink).
	0.96	eIF3Deltah-derived subcomplexes isolated using tagged f or m were entirely missing the right arm (eIF3e) and right leg (eIF3k and l) (Figure 3B), consistent with previous subunit mapping of human eIF3.
	0.96	eIF3e is dispensable for eIF3 assembly (Figures 1B, 1C, and 3B), these data suggest that the C-terminal helices of eIF3a play a more significant role than those of eIF3c in helical bundle formation and suggest that eIF3c assembles into the helical bundle downstream of or concurrently with eIF3a.
	0.95	eIF3e allowed formation of a stable dimer with subunit d, but prevented eIF3e from integrating into the full eIF3 complex (eIF3e 1-418; Figures S2F and S3F).
	0.94	eIF3e levels in the cell would prevent eIF3d from assembling with eIF3, where it might localize to the nucleus as seen in certain cancers or activate or repress the translation of certain cell-proliferation transcripts.
	0.94	eIF3d with eIF3e is indicated, but is not dependent on the C-terminal helices of eIF3e.
	0.93	eIF3 primarily through its highly conserved helical bundle (Figure S4F) and additional contacts with subunits c and l would form only after eIF3e is docked into the helical bundle.
	0.93	eIF3 bound to the 40S subunit and the observed binding of eIF3d 1-114 to eIF3e suggests that eIF3d bridges eIF3e to the 40S subunit in an extended conformation.
	0.92	eIF3e and l) as a dimer, followed by Rpn8 (eIF3k paralog), rather than Rpn3 and 8 (eIF3k and l) as we see with eIF3.
	0.85	eIF3e could directly interact with the N-terminal region of eIF3d (eIF3d 1-114).
	0.82	eIF3 complex and requires the C-terminal helices of eIF3e for assembly into eIF3.
	0.80	eIF3e individually may be responsible for the difference between N. crassa and humans, transiently expressed FLAG-tagged eIF3d was able to pull down endogenous eIF3e in IPs (Figure 4E).
	0.79	eIF3e in complex with subunit d into eIF3 would follow that of subunit h, but precede binding of subunits k and l.
	0.71	eIF3 lacking eIF3l or eIF3e also resulted in the absence of subunits eIF3k or eIF3d, respectively.
	0.57	eIF3d are predicted to be mostly unstructured or in beta-sheet conformations, consistent with an extended interaction between eIF3e and the eIF3d (1-114) suggested by cryo-EM difference maps between eIF3 with and without eIF3d.
28981723	0.97	eIF3d subunit attaches to eIF3 via eIF3e (Figure 3A).
	0.95	eIF3e and eIF3d that attaches eIF3d to the rest of eIF3.
	0.94	eIF3e, which is essential in higher eukaryotes, was also suggested to promote translation of metabolic mRNAs, the authors proposed that eIF3:via its eIF3d-eIF3e module:might orchestrate an mRNA-specific translational mechanism controlling energy metabolism that could be disrupted in cancer.
	0.94	eIF3e is significantly underexpressed, the expression of eIF3d, eIF3k and eIF3l is also dramatically reduced.
	0.92	eIF3e and eIF3d subunits failed to synthesize components of the mitochondrial electron transport chain, leading to a defect in respiration, endogenous oxidative stress, and premature aging.
	0.89	eIF3d or eIF3l-k or eIF3e-d-l-k or eIF3h-l-k subunits.
20462454	0.97	eIF3d, eIF3e, eIF3f and eIF3h are present in mammals, plants and in the fission yeast Schizosaccharomyces pombe, but is absent in S. cerevisiae.
29254951	0.97	eIF3D and eIF3E by both IPO4 and IPO5; Fig EV3B and C).
31281727	0.97	eIF3d, eIF3e, eIF3g and eIF3h) modulate the growth, survival and transformation of breast cancer cells.
15904532	0.96	eIF3d and eIF3e, were conspicuously absent (Fig. 1B, Table 1).
	0.96	eIF3e and its binding partner eIF3d.
	0.80	eIF3e and eIF3d.
	0.79	eIF3d/eIF3e/Rpn5p interaction is either unstable under our purification conditions or contains only a minor fraction of the total eIF3e engaged in protein interactions.
	0.69	eIF3d was readily detectable in the eIF3e complex, it was undetectable in the eIF3m complex (Fig. 3B).
31863585	0.96	eIF3d, it is located more on the eIF3 periphery and is attached to the octamer through eIF3e.
	0.94	eIF3d is sitting on the 40S head in a considerable distance from eIF3e, which forms a so-called right arm of eIF3 not in a direct contact with the 40S.
	0.72	eIF3d extends from the 40S head towards the core of the eIF3 octamer where it interacts with the PCI domain of eIF3e, as well as with eIF3a and eIF3c, we propose that eIF3d creates yet another connecting bridge between the octamer and the 40S.
20016281	0.96	eIF3e and Moe1/eIF3d are also components of eIF3 in S. pombe and in higher eukaryotes.
26399914	0.96	EIF3D and EIF3G are all associated with Liver Failure, Acute Hepatitis; EIF3E, EIF3F and EIF3K are associated with Liver Neoplasms; EIF3H is associated with Carcinoma Hepatocellular; EIF3I is associated with clonorchiasis.
30515407	0.96	EIF3D (x7.2, FDR=0.02), EIF3E (x3.9, FDR=0.0004), EIF3F (x76.9, FDR=0.0009), EIF3G (x12, FDR<0.0001), EIF3H (x6.2, FDR<0.0001), EIF3I (x2.4, FDR=0.02), EIF3J (x25.3, FDR<0.0001), EIF3K (x3.5, FDR=0.003), EIF3L (x5.1, FDR<0.0001), EIF3M (x6.6, FDR<0.0001), EIF4A3 (x24.9, FDR=0.009), EIF4E (x-3.4, FDR=0.001), EIF4G1 (x-2.4, FDR=0.02), EIF4G2 (x-2.1, FDR=0.004), EIFG3 (x-2.66, FDR=0.003), and EIF5B (x2.8, FDR=0.005).
31239291	0.96	EIF3D and EIF3E).
28083147	0.95	eIF3d-eIF3e in maintaining mitochondrial respiration components and serving to adjust metabolic pathways may help us better understand how the cancer-promoting properties of the eIF3 complex emerge.
	0.93	eIF3e triggers a metabolic switch that increases dependence on glycolysis, as respiratory deficiencies alongside increased sensitivity to oxidative stress are also observed when eIF3d is depleted in addition to eIF3e knockdown.
	0.89	eIF3d, eIF3e, eIF3h, and eIF3i along with reduced levels of eIF3e and eIF3f has been observed in several cancers (Table 1).
	0.88	eIF3d-eIF3e module within the eIF3 complex that regulates the translation of specific mRNAs involved in maintaining metabolic pathways that are likely disrupted in cancer cells.
19818717	0.93	eIF3d and eIF3e are peripheral subunits that may undergo dynamic exchange, although the signals that can trigger such exchange remain to be identified.
	0.89	eIF3d and eIF3e can be readily purified from unstressed S. pombe cells (Fig. 1, Fig. 2) as well as from other organisms, these proteins may also carry out important, albeit non-essential, functions under normal growth conditions.
	0.86	eif3d and eif3e mutants are sensitive.
	0.74	eIF3e is readily detected in the nucleus, when eif3d/moe1 is deleted; conversely, eIF3d becomes nuclear, when eif3e is missing.
21173787	0.93	EIF3D, EIF3E, EIF3F, EIF3H, EIF3I, EIF4A1, EIF4A3, EIF4B, EIF4EBP1, EIF5, EIF5B).
31171919	0.93	eIF3d, eIF3e, eIF3f, eIF3h and eIF3l highly were associated with the IDH mutant status of gliomas.
22941651	0.92	EIF3D, EIF3E, EIF4G2, EIF5B and EEF2), were marked by SUMO-1 at their promoters during interphase and had mRNA expression stimulated by SUMO-1.
28088948	0.92	eIF3d, and eIF3e for eIF4G and eIF3g for CTIF).
25539953	0.91	eIF3d, eIF3e, eIF3h, eIF3k and eIF3l) and appears to have suffered a drastic reduction in complexity during its evolution.
	0.83	eIF3d and eIF3e) whilst in yeast this is done indirectly, through eIF5 .
21364753	0.90	EIF3D, EIF3E, EIF3F, EIF3H).
30416377	0.89	eIF3d, eIF3e, eIF3f, eIF3g, eIF3h, eIF3i, eIF3j, eIF3k, eIF3l, and eIF3m. eIF3a, eIF3c, eIF3e, eIF3k, eIF3l, and eIF3m, which contain a PCI (proteasome, COP9/signalosome, eIF3) domain, and eIF3f, and eIF3h, which have an MPN (Mpr1-Pad1-N-terminal) domain, make up the octameric structural core of eIF3.
20816988	0.86	eIF3d, eIF3e, eIF3f, eIF3h, and eIF3m. Notably, the predicted size of the eIF3 complexes in peak 3 (~300-400 kDa) is not consistent with all of the identified subunits being present in a unique complex.
29401259	0.86	eIF3e, eIF3h, eIF3l) cross-link with each other and with eIF3d which is in proximity (Figures 4A and 3A).
29635389	0.86	eIF3d and eIF3e form a module that is incorporated to the eIF3 complex in the late steps of assembly, and that depletion of eIF3e leads to co-depletion of eIF3d in Hela cells.
26344199	0.84	eIF3e, but recent analysis revealed a second, adjacent site on eIF4G that binds to eIF3c and eIF3d.
29725087	0.61	eIF3d and eIF3e subunits, thereby recruiting the 43S PIC to the cap.
26984530	0.54	eIF3e (right arm), eIF3c (head) and eIF3d subunits interact with eIF4G-M to promote the attachment of the eIF4F-mRNA complex to the mammalian 43S complex.
20503360	0.52	eIF3d, eIF3e, eIF3f, and eIF3h and these subunits have been shown to be integral components of the purified eIF3 protein complex.
27924037	0.52	eIF3e resulted in simultaneous, severe downregulation of the protein levels of subunits within the entire right side of the eIF3 octamer body: the right leg subunits eIF3k and eIF3l, as well as the non-octameric eIF3d subunit (Figure 3E, Supplementary Figure S4E, and Table 1).