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Gene Review

Eif4g1  -  eukaryotic translation initiation factor 4...

Mus musculus

Synonyms: E030015G23Rik, Eukaryotic translation initiation factor 4 gamma 1, eIF-4-gamma 1, eIF-4G 1, eIF-4G1, ...
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Disease relevance of Eif4g1


High impact information on Eif4g1

  • In addition, both Pdcd4 and Pdcd4(D418A) bound to the middle region of eIF4G [4].
  • It has been proposed that binding of the eukaryotic translation initiation factor 4E (eIF-4E) to the inhibitory protein 4BP-1 blocks translation by preventing access of eIF-4G to the 5' cap of the mRNA [5].
  • The cleavage of eIF4GI, which specifically needs caspase-3 activity, is dispensable for the inhibition of translation in MCF-7 cells [6].
  • In addition, the stimulatory effect of eIF4G on the cap recognition of eIF4E is inhibited by the translational repressor, 4E-BP1 [7].
  • Activation of a temperature-sensitive form of mouse p53 in murine erythroleukaemia cells rapidly inhibits protein synthesis and causes early dephosphorylation and cleavage of protein synthesis initiation factor eIF4GI and the eIF4E-binding protein 4E-BP1 [8].

Biological context of Eif4g1

  • The signal for translation initiation is thought to involve phosphorylation of 4BP-1, which causes it to dissociate from eIF-4E and allows eIF-4G to localize to the 5' cap [5].
  • This synergy is mediated via interactions between eIF4G (a component of the eIF4F cap binding complex) and poly(A) binding protein (PABP) [9].
  • NAC and DPI also inhibited phosphorylation of 4E-BP1 on Thr46 and association of eIF4E with eIF4G, steps that are important in the initiation phase of mRNA translation [10].
  • Both full-length and N-terminally truncated eIF4G transfectants of NIH3T3 cells formed colonies in soft agar and increased the saturation density of cell growth, indicating that both eIF4Gs function similarly [11].
  • The inhibition of translation is associated with specific cleavages of polypeptide chain initiation factors eIF4GI and eIF4B, a phenomenon previously observed in cells induced to undergo apoptosis in response to other stimuli [12].

Anatomical context of Eif4g1

  • When bound to 4E-BP1, eIF4E cannot bind to eIF4G to form the active eIF4F complex, an event that is required for the binding of mRNA to the ribosome [13].
  • All of the retroviral proteases examined were able to cleave the initiation factor eIF4GI both in intact cells and in cell-free systems, albeit with different efficiencies [3].

Associations of Eif4g1 with chemical compounds

  • The amount of serine 1108-phosphorylated eIF4G (but not Ser209-phosphorylated eIF4E) was induced following PH [14].
  • Leucine also increased the association of the initiation factors eIF4E and eIF4G, but did not affect the activity of the guanine nucleotide exchange factor eIF2B, nor total protein synthesis [15].

Physical interactions of Eif4g1

  • Enhancement of the eIF4E affinity for cap occurs after binding to eIF4G peptides [16].

Other interactions of Eif4g1

  • Insulin and IGF-I increased the amount of eIF4G associated with eIF4E in nutrient-deprived C2C12 myotubes [17].
  • Caerulein inhibited the two major regulatory points of translation initiation: the activity of the guanine nucleotide exchange factor eIF2B (with an increase of eIF2alpha phosphorylation) and the formation of the eIF4F complex due, in part, to degradation of eIF4G [18].
  • The role of eIF4G during the initiation of protein synthesis was studied using mouse mammary carcinoma FM3A cells and FM4G cells that overproduce an N-terminally truncated form of eIF4G, which lacks the binding site of poly(A)-binding protein [11].
  • The Pdcd4 protein has weak homology to the eucaryotic translation initiation factor eIF4G and has been shown to interact with certain translation initiation factors [19].
  • In addition, eIF2B epsilon, eIF4G1, and p70 S6 kinase protein levels decreased progressively with increasing recirculation time [20].


  1. Sequential modification of translation initiation factor eIF4GI by two different foot-and-mouth disease virus proteases within infected baby hamster kidney cells: identification of the 3Cpro cleavage site. Strong, R., Belsham, G.J. J. Gen. Virol. (2004) [Pubmed]
  2. Acute treatment with TNF-alpha attenuates insulin-stimulated protein synthesis in cultures of C2C12 myotubes through a MEK1-sensitive mechanism. Williamson, D.L., Kimball, S.R., Jefferson, L.S. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  3. The eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases. Alvarez, E., Menéndez-Arias, L., Carrasco, L. J. Virol. (2003) [Pubmed]
  4. The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Yang, H.S., Jansen, A.P., Komar, A.A., Zheng, X., Merrick, W.C., Costes, S., Lockett, S.J., Sonenberg, N., Colburn, N.H. Mol. Cell. Biol. (2003) [Pubmed]
  5. Cell cycle progression and proliferation despite 4BP-1 dephosphorylation. Marx, S.O., Marks, A.R. Mol. Cell. Biol. (1999) [Pubmed]
  6. Inhibition of protein synthesis in apoptosis: differential requirements by the tumor necrosis factor alpha family and a DNA-damaging agent for caspases and the double-stranded RNA-dependent protein kinase. Jeffrey, I.W., Bushell, M., Tilleray, V.J., Morley, S., Clemens, M.J. Cancer Res. (2002) [Pubmed]
  7. eIF4G dramatically enhances the binding of eIF4E to the mRNA 5'-cap structure. Haghighat, A., Sonenberg, N. J. Biol. Chem. (1997) [Pubmed]
  8. Regulation of the phosphorylation and integrity of protein synthesis initiation factor eIF4GI and the translational repressor 4E-BP1 by p53. Constantinou, C., Clemens, M.J. Oncogene (2005) [Pubmed]
  9. Regulation of poly(A) binding protein function in translation: Characterization of the Paip2 homolog, Paip2B. Berlanga, J.J., Baass, A., Sonenberg, N. RNA (2006) [Pubmed]
  10. Angiotensin II stimulation of VEGF mRNA translation requires production of reactive oxygen species. Feliers, D., Gorin, Y., Ghosh-Choudhury, G., Abboud, H.E., Kasinath, B.S. Am. J. Physiol. Renal Physiol. (2006) [Pubmed]
  11. Increase in cap- and IRES-dependent protein synthesis by overproduction of translation initiation factor eIF4G. Hayashi, S., Nishimura, K., Fukuchi-Shimogori, T., Kashiwagi, K., Igarashi, K. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  12. p53-induced inhibition of protein synthesis is independent of apoptosis. Constantinou, C., Bushell, M., Jeffrey, I.W., Tilleray, V., West, M., Frost, V., Hensold, J., Clemens, M.J. Eur. J. Biochem. (2003) [Pubmed]
  13. A microtiter plate assay for assessing the interaction of eukaryotic initiation factor eIF4E with eIF4G and eIF4E binding protein-1. Kimball, S.R., Horetsky, R.L., Jefferson, L.S. Anal. Biochem. (2004) [Pubmed]
  14. Rapamycin-sensitive induction of eukaryotic initiation factor 4F in regenerating mouse liver. Goggin, M.M., Nelsen, C.J., Kimball, S.R., Jefferson, L.S., Morley, S.J., Albrecht, J.H. Hepatology (2004) [Pubmed]
  15. Leucine activates pancreatic translational machinery in rats and mice through mTOR independently of CCK and insulin. Sans, M.D., Tashiro, M., Vogel, N.L., Kimball, S.R., D'Alecy, L.G., Williams, J.A. J. Nutr. (2006) [Pubmed]
  16. Biophysical studies of eIF4E cap-binding protein: recognition of mRNA 5' cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins. Niedzwiecka, A., Marcotrigiano, J., Stepinski, J., Jankowska-Anyszka, M., Wyslouch-Cieszynska, A., Dadlez, M., Gingras, A.C., Mak, P., Darzynkiewicz, E., Sonenberg, N., Burley, S.K., Stolarski, R. J. Mol. Biol. (2002) [Pubmed]
  17. Insulin and IGF-I stimulate the formation of the eukaryotic initiation factor 4F complex and protein synthesis in C2C12 myotubes independent of availability of external amino acids. Shen, W.H., Boyle, D.W., Wisniowski, P., Bade, A., Liechty, E.A. J. Endocrinol. (2005) [Pubmed]
  18. Caerulein-induced acute pancreatitis inhibits protein synthesis through effects on eIF2B and eIF4F. Sans, M.D., DiMagno, M.J., D'Alecy, L.G., Williams, J.A. Am. J. Physiol. Gastrointest. Liver Physiol. (2003) [Pubmed]
  19. The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA. Böhm, M., Sawicka, K., Siebrasse, J.P., Brehmer-Fastnacht, A., Peters, R., Klempnauer, K.H. Oncogene (2003) [Pubmed]
  20. Mechanisms underlying suppression of protein synthesis induced by transient focal cerebral ischemia in mouse brain. Mengesdorf, T., Proud, C.G., Mies, G., Paschen, W. Exp. Neurol. (2002) [Pubmed]
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