Regulation of protein synthesis and the role of eIF3 in cancer

Hershey, John W.B.

doi:10.1590/s0100-879x2010007500098

Cited by 43 publications

(37 citation statements)

References 56 publications

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“…Although eIF3b is highly expressed in several forms of cancer (52)(53)(54)(55) and its down-regulation has been shown to inhibit the proliferation and metastatic potential of colon, bladder, and prostate cancers (52,53), little is known about eIF3b function(s) at the molecular level. Previous research indicated that eIF3b serves as a binding scaffold for the other core subunits and for eIF2 (47, 49 -51), whereas its interaction with eIF3a, eIF3j, and eIF1a ensures proper formation of the scanning-arrested conformation required for stringent AUG recognition (56).…”

Section: Discussionmentioning

confidence: 99%

Novel RNA-binding Protein P311 Binds Eukaryotic Translation Initiation Factor 3 Subunit b (eIF3b) to Promote Translation of Transforming Growth Factor β1-3 (TGF-β1-3)

Yue¹,

Lv²,

Meredith

et al. 2014

Journal of Biological Chemistry

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Background: P311 is a stimulator of TGF-␤1-3 translation, but its mechanism of action is unknown. Results: P311 binds eIF3b and the 5ЈUTRs of TGF-␤1-3 mRNAs. Thereby, P311 recruits TGF-␤1-3 mRNAs to the translation machinery. Conclusion: P311 is an RNA-binding protein that binds to eIF3b to stimulate TGF-␤1-3 translation. Significance: Our studies add a new level of complexity to TGF-␤ signaling regulation.

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Section: Discussionmentioning

confidence: 99%

Novel RNA-binding Protein P311 Binds Eukaryotic Translation Initiation Factor 3 Subunit b (eIF3b) to Promote Translation of Transforming Growth Factor β1-3 (TGF-β1-3)

Yue¹,

Lv²,

Meredith

et al. 2014

Journal of Biological Chemistry

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“…The human INT6 protein was further identified as a target of the Human T-cell Leukaemia Virus type 1 (HTLV-1) transforming protein Tax (Desbois et al 1996) and also as the EIF3E subunit of the eIF3 translation initiation factor (Asano et al 1997). EIF3 establishes multiple contacts with other translation initiation factors like eIF1A, eIF5, and eIF4G (Hinnebusch 2006;Hershey 2010). It also binds the mRNA, the 40S ribosome subunit, and favors association with the ternary complex, thereby playing a key role in translation initiation.…”

Section: Introductionmentioning

confidence: 99%

INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation

Neusiedler¹,

Mocquet²,

Limousin³

et al. 2012

RNA

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The INT6/EIF3E protein has been implicated in mouse and human breast carcinogenesis. This subunit of the eIF3 translation initiation factor that includes a PCI domain exhibits specific features such as presence in the nucleus and ability to interact with other important cellular protein complexes like the 26S proteasome and the COP9 signalosome. It has been previously shown that INT6 was not essential for bulk translation, and this protein is considered to regulate expression of specific mRNAs. Based on the results of a two-hybrid screen performed with INT6 as bait, we characterize in this article the MIF4GD/SLIP1 protein as an interactor of this eIF3 subunit. MIF4GD was previously shown to associate with SLBP, which binds the stem-loop located at the 39 end of the histone mRNAs, and to be necessary for efficient translation of these cell cycle-regulated mRNAs that lack a poly(A) tail. In line with the interaction of both proteins, we show using the RNA interference approach that INT6 is also essential to S-phase histone mRNA translation. This was observed by analyzing expression of endogenous histones and by testing heterologous constructs placing the luciferase reporter gene under the control of the stem-loop element of various histone genes. With such a reporter plasmid, silencing and overexpression of INT6 exerted opposite effects. In agreement with these results, INT6 and MIF4GD were observed to colocalize in cytoplasmic foci. We conclude from these data that INT6, by establishing interactions with MIF4GD and SLBP, plays an important role in translation of poly(A) minus histone mRNAs.

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“…The ribosome is recruited by eIF4E to carry out the on-going process of polypeptide synthesis in what is called steady-state translation, responsible for the bulk protein synthesis. We will hereafter refer to this process as eIF4E-dependent translation (ET) (8,9).…”

mentioning

confidence: 99%

“…Mammalian eIF3 consists of at least 13 different polypeptides that are designated eIF3a to eIF3m depending on their protein mass (8,9). The eIF3 complex plays multiple roles in translation by (i) stabilizing the 40S ribosomal subunit; (ii) promoting the formation of the 43S pre-initiation complex; (iii) enhancing ribosome recruitment to mRNA via interactions with other eIFs; and (iv) helping ribosome scanning for re-initiation (8,9,15).…”

mentioning

confidence: 99%

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

Choe

Park

et al. 2012

Journal of Biological Chemistry

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Background: How the eIF3 complex and ribosomes are recruited during translation on CBP80/20-bound mRNAs remains obscure. Results: CTIF interacts with eIF3g to recruit the eIF3 complex. Conclusion: Translation on CBP80/20-bound mRNAs requires CTIF-eIF3g interaction. Significance: The use of different eIF3 subunits for recruiting eIF3 complex implies that translation on CBP80/20-bound mRNAs differs mechanistically from translation on eIF4E-bound mRNAs.

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Regulation of protein synthesis and the role of eIF3 in cancer

Cited by 43 publications

References 56 publications

Novel RNA-binding Protein P311 Binds Eukaryotic Translation Initiation Factor 3 Subunit b (eIF3b) to Promote Translation of Transforming Growth Factor β1-3 (TGF-β1-3)

Novel RNA-binding Protein P311 Binds Eukaryotic Translation Initiation Factor 3 Subunit b (eIF3b) to Promote Translation of Transforming Growth Factor β1-3 (TGF-β1-3)

INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation

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

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