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Review
. 2018 Sep 7;14(12):1630-1635.
doi: 10.7150/ijbs.26932. eCollection 2018.

The Biological Roles of Translation Initiation Factor 3b

Affiliations
Review

The Biological Roles of Translation Initiation Factor 3b

Xuefei Feng et al. Int J Biol Sci. .

Abstract

Translation has important roles in almost all physiological and pathological processes, and translation initiation factors are particularly relevant to the translation initiation step, which is the most important step in translation regulation. Translation initiation factor 3b (eIF3b), a key subunit of the largest translation initiation factor 3 (eIF3), is widely considered a scaffold protein that acts to ensure the accuracy of translation initiation. A series of recent finds has revealed that eIF3 is closely related to oncogenesis. However, the concrete mechanism by which eIF3b is involve in carcinogenesis remains elusive. Here, we summarize a series of research findings regarding the relationship between eIF3b, translation and cancer.

Keywords: cancer.; eIF3b; translation initiation.

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Conflict of interest statement

Competing Interests: The authors have declared that no competing interest exists.

Figures

Fig 1
Fig 1
The functions of eIF3.
Fig 2
Fig 2
Structure of YLC.
Fig 3
Fig 3
Domains of eIF3b protein in mammals and budding yeast.
Fig 4
Fig 4
The association of eIF3b and cancer.

References

    1. Saletta F, Suryo Rahmanto Y, Richardson DR. The translational regulator eIF3a: the tricky eIF3 subunit! Biochimica et biophysica acta. 2010;1806:275–86. - PubMed
    1. des Georges A, Dhote V, Kuhn L, Hellen CU, Pestova TV, Frank J. et al. Structure of mammalian eIF3 in the context of the 43S preinitiation complex. Nature. 2015;525:491–5. - PMC - PubMed
    1. Hashem Y, des Georges A, Dhote V, Langlois R, Liao HY, Grassucci RA. et al. Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29. Cell. 2013;153:1108–19. - PMC - PubMed
    1. Hashem Y, des Georges A, Dhote V, Langlois R, Liao HY, Grassucci RA. et al. Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit. Nature. 2013;503:539–43. - PMC - PubMed
    1. Sun C, Todorovic A. et al. Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3) PNAS. 2011;108:20473–8. - PMC - PubMed

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