Conducting the initiation of protein synthesis: the role of eIF4G

Prévot, Danielle; Darlix, Jean‐Luc; Ohlmann, Théophile

doi:10.1016/s0248-4900(03)00031-5

Cited by 199 publications

(94 citation statements)

References 151 publications

(202 reference statements)

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“…In TbG1 five phosphorylated serines and one tyrosine have been detected (Urbaniak et al 2013). TbG2, which has a human eIF4G counterpart with a scaffold function (Prévôt et al 2003), has three phosphorylated serines and two phosphorylated threonines (Urbaniak et al 2013), making it the best candidate for 14-3-3 binding.…”

Section: Discussionmentioning

confidence: 99%

“…While the reciprocal scenario of multiple eIF4E proteins binding a single eIF4G scaffold has been documented (Prévôt et al 2003;Clarkson et al 2010), the TbE5 situation is notable. Furthermore, the associates of each complex are distinct, implying that the two complexes could perform unique regulatory functions.…”

Section: Tbeif4e5 Associates With Two Distinct Sub-complexesmentioning

confidence: 99%

“…The yeast Saccharomyces cerevisiae possesses a single eIF4E and two eIF4Gs with distinct functions (Prévôt et al 2003;Clarkson et al 2010); humans have four eIF4E isoforms and two eIF4Gs (Prévôt et al 2003;Joshi et al 2004). The nematode Caenorhabditis elegans, in contrast, possesses five eIF4E variants (Keiper et al 2000) that displays distinct preferences for m 7 G and m 2,2,7 G cap structures (JankowskaAnyszka et al 1998), and a single eIF4G gene that gives rise to two isoforms (Contreras et al 2008).…”

Section: Introductionmentioning

confidence: 99%

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eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

Freire

Vashisht

Malvezzi

et al. 2014

RNA

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Members of the eIF4E mRNA cap-binding family are involved in translation and the modulation of transcript availability in other systems as part of a three-component complex including eIF4G and eIF4A. The kinetoplastids possess four described eIF4E and five eIF4G homologs. We have identified two new eIF4E family proteins in Trypanosoma brucei, and define distinct complexes associated with the fifth member, TbEIF4E5. The cytosolic TbEIF4E5 protein binds cap 0 in vitro. TbEIF4E5 was found in association with two of the five TbEIF4Gs. TbIF4EG1 bound TbEIF4E5, a 47.5-kDa protein with two RNA-binding domains, and either the regulatory protein 14-3-3 II or a 117.5-kDa protein with guanylyltransferase and methyltransferase domains in a potentially dynamic interaction. The TbEIF4G2/TbEIF4E5 complex was associated with a 17.9-kDa hypothetical protein and both 14-3-3 variants I and II. Knockdown of TbEIF4E5 resulted in the loss of productive cell movement, as evidenced by the inability of the cells to remain in suspension in liquid culture and the loss of social motility on semisolid plating medium, as well as a minor reduction of translation. Cells appeared lethargic, as opposed to compromised in flagellar function per se. The minimal use of transcriptional control in kinetoplastids requires these organisms to implement downstream mechanisms to regulate gene expression, and the TbEIF4E5/TbEIF4G1/117.5-kDa complex in particular may be a key player in that process. We suggest that a pathway involved in cell motility is affected, directly or indirectly, by one of the TbEIF4E5 complexes.

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Section: Discussionmentioning

confidence: 99%

Section: Tbeif4e5 Associates With Two Distinct Sub-complexesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

Freire

Vashisht

Malvezzi

et al. 2014

RNA

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“…Mammalian eIF4F complexes contain eIF4A, the prototype of the DEAD box helicase family (7,8); however, plant eIF4A is loosely associated and is easily removed during purification (9). eIF4G is a multifunctional protein that is an important structural platform for the assembly or nucleation of several initiation factors (eIF4A, eIF3, eIF4B, eIF5, and poly(A)-binding protein) and interaction with the 40 S ribosome during the initiation process (10,11). Furthermore, in mammals there is also interaction of eIF4G with MNK kinase that then phosphorylates associated eIF4E (12).…”

mentioning

confidence: 99%

Plant Cap-binding Complexes Eukaryotic Initiation Factors eIF4F and eIFISO4F

Mayberry

Allen

Nitka

et al. 2011

Journal of Biological Chemistry

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Background: Plants have a unique form of cap-binding complex. Results: Correct and mixed complexes show differential translation, and mixed complex subunits have lower binding affinity than correct complex subunits. Conclusion:The subunits of the cap-binding complexes show specificity for complex formation, and the translational efficiency is determined by the large subunit. Significance: The results suggest the potential for differential translation by the two plant cap-binding complexes.

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“…Hence, the interaction of eIF4G and 4E-BP with eIF4E is mutually exclusive (Haghighat et al 1995). eIF4G scaffold proteins such as eIF4A, an RNA helicase which unwinds secondary structures in mRNA 5 0 -UTRs that may otherwise impede scanning of the initiator codon by the 43S pre-initiation complex (Prevot et al 2003). Phosphorylation of eIF4G by unidentified, mTOR-dependent kinases facilitates its activity (Raught et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Activation of a GPCR leads to eIF4G phosphorylation at the 5′ cap and to IRES-dependent translation

Leon¹,

Boulo²,

Musnier³

et al. 2014

Journal of Molecular Endocrinology

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The control of mRNA translation has been mainly explored in response to activated tyrosine kinase receptors. In contrast, mechanistic details on the translational machinery are far less available in the case of ligand-bound G protein-coupled receptors (GPCRs). In this study, using the FSH receptor (FSH-R) as a model receptor, we demonstrate that part of the translational regulations occurs by phosphorylation of the translation pre-initiation complex scaffold protein, eukaryotic initiation factor 4G (eIF4G), in HEK293 cells stably expressing the FSH-R. This phosphorylation event occurred when eIF4G was bound to the mRNA 5 0 cap, and probably involves mammalian target of rapamycin. This regulation might contribute to cap-dependent translation in response to FSH. The cap-binding protein eIF4E also had its phosphorylation level enhanced upon FSH stimulation. We also show that FSH-induced signaling not only led to cap-dependent translation but also to internal ribosome entry site (IRES)-dependent translation of some mRNA. These data add detailed information on the molecular bases underlying the regulation of selective mRNA translation by a GPCR, and a topological model recapitulating these mechanisms is proposed.

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Conducting the initiation of protein synthesis: the role of eIF4G

Cited by 199 publications

References 151 publications

eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei

Plant Cap-binding Complexes Eukaryotic Initiation Factors eIF4F and eIFISO4F

Activation of a GPCR leads to eIF4G phosphorylation at the 5′ cap and to IRES-dependent translation

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