ライフサイエンスコーパス: eIF4G

1 eIF4G binding to the eIF4E-m(7)GTP cap complex is resist

2 eIF4G is an essential translation factor that exerts str

3 eIF4G is the major adaptor subunit of eIF4F that binds t

4 eIF4G is the scaffold subunit of the eIF4F complex, whos

5 eIF4G/eIF4A then restructure the region of ribosomal att

6 rly, a C-terminal fragment of human eIF4G-1, eIF4G(1357-1600), which prevents binding of MNK to intac

7 Together with eIF3 and eIF4A/4B, eIF4G recruits ribosomal subunits to mRNAs and facilitat

8 ryotic initiation factors 4E (eIF4E) and 4G (eIF4G) reduces the enhancement of L-LTP induction brough

9 ion between eukaryotic initiation factor 4G (eIF4G) and eIF3 is thought to act as the molecular bridg

10 eukaryotic translation initiation factor 4G (eIF4G) and phosphorylates the cap-binding protein eIF4E.

11 eukaryotic translation initiation factor 4G (eIF4G) and the Lys-rich segment (K-boxes) of eIF2beta bi

12 ing site in eukaryotic initiation factor 4G (eIF4G) functions as an autoinhibitory domain to modulate

13 teract with eukaryotic initiation factor 4G (eIF4G) were required to observe maximal repression by Pu

14 sm requires eukaryotic initiation factor 4G (eIF4G), subunit of heterodimer eIF4F (plant eIF4F lacks

15 eukaryotic translation initiation factor 4G (eIF4G), the scaffold subunit of eukaryotic translation i

16 eukaryotic translation initiation factor 4G (eIF4G), we investigated whether Unr has a general role i

17 on initiation apparatus and ribosome adaptor eIF4G.

18 ins (m4E-BPs) advantageously compete against eIF4G via bimodal interactions involving this canonical

19 Third, mutations altering eIF4G-RS1, eIF2beta-K-boxes, and eIF5-CTD restore the ac

20 Finally, by employing an eIF4G-dependent translation assay, we establish that bot

21 at yeast Fal1p interacts genetically with an eIF4G-like protein, Sgd1p: One allele of sgd1 acts as a

22 binding motif, varies between each 4E-BP and eIF4G.

23 We observed that 4E-BP1 and eIF4G bind eIF4E at similar levels during interphase and

24 lated by two disordered proteins, 4E-BP1 and eIF4G, that inhibit or stimulate the activity of the m(7

25 l association of mRNAs for p 120 catenin and eIF4G.

26 m(7)GTP-Sepharose reveals that both CGP and eIF4G(1357-1600) decrease binding of eIF4E to eIF4G.

27 articular, the interaction between eIF4A and eIF4G is destabilized, leading to a temporary stabilizat

28 ensure efficient duplex unwinding, eIF4B and eIF4G cooperatively activate the duplex unwinding activi

29 4E with an allosteric inhibitor of eIF4E and eIF4G binding, 4EGI-1, decreased the eIF4E/eIF4G express

30 Translation factors eIF4E and eIF4G form eIF4F, which interacts with the messenger RNA

31 sites (IRES) that are sensitive to eIF4E and eIF4G levels.

32 ic translation initiation factors, eIF4E and eIF4G or their isoforms.

33 ate levels accompanied the rise in eIF4E and eIF4G protein levels, the overall abundance of PABP mRNA

34 t maintaining a connection between eIF4E and eIF4G throughout scanning provides a plausible mechanism

35 of translation initiation factors eIF4E and eIF4G to p63alpha mRNA.

36 eIF4E and the interaction between eIF4E and eIF4G.

37 on to yield free subunits (eIF4A, eIF4E, and eIF4G) is presented.

38 cap by the eIF4F complex (eIF4A, eIF4E, and eIF4G).

39 ressed by blocking assembly of the eIF4F and eIF4G complex to the mRNA 5' cap.

40 dependence between the two RNA helicases and eIF4G, and suggest that Ded1p is an integral part of eIF

41 F4A, and we demonstrate that Gle1(InsP6) and eIF4G both activate their DEAD-box partner by stimulatin

42 oop, matches an element in type 1 IRESs, and eIF4G-binding motifs in domain K and in type 2 IRESs are

43 they encode multiple eIF4E (LeishIF4Es) and eIF4G (LeishIF4Gs) paralogs, as each could be assigned a

44 nslation initiation such as eIF4E, mTOR, and eIF4G have been shown to induce a malignant phenotype.

45 ally increased by equol was the oncogene and eIF4G enhancer, c-Myc.

46 ering with the interaction between Pab1p and eIF4G.

47 ired for the stable interaction of PABP1 and eIF4G in cells.

48 7-methylguanosine cap of messenger RNA, and eIF4G, which serves as a scaffold to recruit other trans

49 me entry site (IRES), ribosome shunting, and eIF4G enhancers.

50 by single-cell nascent protein synthesis and eIF4G RNA immunoprecipitation sequencing.

51 finity interaction occurring between VPg and eIF4G.

52 n number and organization to those of animal eIF4G.

53 Loss of any eIF4G isoform also resulted in a substantial reduction i

54 lly distinct, although it contains an apical eIF4G-interacting motif similar to that in Type 2 IRESs.

55 Well-known examples are eIF4G and Gle1, which bind and activate the DEAD-box pro

56 the eIF4G isoforms in plants, referred to as eIF4G and eIFiso4G, are highly divergent in size, sequen

57 role in stabilizing the interaction between eIF4G and eIF3.

58 proteins, Npl3 and Sbp1, also directly bind eIF4G and repress translation in a manner dependent on t

59 IF3e subunit has been shown to directly bind eIF4G, but the potential role of other eIF3 subunits in

60 hat eIF4E1b and eIF4E1c are unlikely to bind eIF4G in vivo when in competition with eIF4E.

61 h m(7)GTP-Sepharose and, rather than binding eIF4G, interacted with 4E-T.

62 Whereas dV binds eIF4G, a conserved AUG in dVI was suggested to stimulate

63 f their eIF3 constituent with the IRES-bound eIF4G.

64 eIF4F complex formation is not required but eIF4G plays a critical role in this translation mechanis

65 tes mRNA recruitment through mRNA binding by eIF4G and eIF2beta and assists the start codon-induced r

66 within the optimal activity zone dictated by eIF4G's mechanistic role.

67 xes and that this interaction is mediated by eIF4G.

68 ubstrate pro-ISG15 while preserving cellular eIF4G cleavage.

69 tegral part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.

70 ore, we detected native complexes containing eIF4G and yeIF4B but lacking eIF4A.

71 phorylation of the Mnk1 active site controls eIF4G binding.

72 Despite detailed eIF4G structure data, the mechanisms controlling initiat

73 We propose that expression of 3e5 diminishes eIF4G interaction with eIF3 and causes abnormal gene exp

74 mplex and alleviate the necessity for direct eIF4G/eIF3 interaction.

75 RNAs inhibit protein synthesis by displacing eIF4G/eIF4A from uncapped > capped RNAs.

76 enyl)]propionic acid), an inhibitor of eFI4E-eIF4G interactions, nor PF-4708671 [2-((4-(5-ethylpyrimi

77 c protein synthesis initiation factors (eIF) eIF4G and eIF4E, were up-regulated in mammary tumors fro

78 ing to a temporary stabilization of the eIF3-eIF4G interaction on the 48S complex.

79 dy reveals unexpected complexity to the eIF3-eIF4G interaction that provides new insight into the reg

80 k for the interactions between Ded1p, eIF4A, eIF4G, RNA and ATP, which indicates that eIF4A, with and

81 All of them require eIF2, eIF3, eIF4A, eIF4G, eIF4B, eIF1A, and a single ITAF, poly(C) binding

82 amalgam of three initiation factors, eIF4A, eIF4G, and eIF4E, by the chemical inhibitor 4E1RCat did

83 ivo, and the rescue of specific mutant eIF4A.eIF4G complexes by yeIF4B was reconstituted in vitro.

84 related with the restoration of native eIF4A.eIF4G complexes in vivo, and the rescue of specific muta

85 eIF4A/eIF4G stimulated initiation only at low temperatures or

86 demonstrates that this novel conserved eIF4A/eIF4G-like complex acts in pre-rRNA processing, adding t

87 adding to the established functions of eIF4A/eIF4G in translation initiation and of eIF4AIII as the c

88 rimposed on the X-ray structure of the eIF4A/eIF4G complex.

89 und eukaryotic initiation factor 4E (eIF4E), eIF4G, and poly(A) tail-binding protein (PABP) that circ

90 tic translation initiation factor 4E (eIF4E)-eIF4G interactions and p70 S6 kinase polypeptide 1 (S6K1

91 cap-eukaryotic initiation factor 4E (eIF4E)-eIF4G-eIF3-40S chain of interactions, but the mechanism

92 presence of the PIC, independently of eIF4E*eIF4G, but dependent on subunits i and g of the heterome

93 d abundance of eIF4F core components (eIF4E, eIF4G, eIF4A) and the eIF4F-associated factor poly(A) bi

94 ociations of the core mRNP components eIF4E, eIF4G, and PABP and of the decay factor DDX6 in human ce

95 y initiation factor complex involving eIF4E, eIF4G, and eIF4A1.

96 ic initiation factor 4F), composed of eIF4E, eIF4G, and eIF4A, binds to the m(7)G cap structure of mR

97 al 'closed loop' complex comprised of eIF4E, eIF4G, and Pab1, and depletion of eIF4G mimics the trans

98 ncreased expression of phosphorylated eIF4E, eIF4G, and eIF4A1 in human and murine skin SCCs.

99 ugs in concert to simultaneously block eIF4E-eIF4G interactions and S6K1 immediately after memory rea

100 on eIF4G peptide and propose the first eIF4E-eIF4G structural model for plants.

101 anonical motifs, similarly to metazoan eIF4E-eIF4G complexes.

102 As in the case of metazoan eIF4E-eIF4G, this may have very important practical implicatio

103 er reactivation, whereas inhibition of eIF4E-eIF4G interactions did not.

104 Omission of eIF4A or disruption of eIF4E-eIF4G-eIF3 interactions converted eIF4E into a specific

105 rtant practical implications, as plant eIF4E-eIF4G is also involved in a significant number of plant

106 in vitro and in vivo evidence that the eIF4E-eIF4G complex is more stringently required for plasticit

107 The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal

108 are consistent with the model in which eIF4E-eIF4G-eIF3-40S interactions place eIF4E at the leading e

109 er, VPg formed trimeric complexes with eIF4E-eIF4G, eIF4E bound VPg-luciferase RNA conjugates, and th

110 DCD4), which sequesters eIF4A from the eIF4E.eIF4G complex, resulting in repressed translation of mRN

111 F4E, thereby promoting assembly of the eIF4E.eIF4G complex.

112 NAs between eIF4E/4E-BP repression and eIF4E/eIF4G translation initiation.

113 A recently discovered small molecule, eIF4E/eIF4G interaction inhibitor 1 (4EGI-1), disrupts the eIF

114 4EGI-1 is the prototypic inhibitor of eIF4E/eIF4G interaction, a potent inhibitor of translation ini

115 totypic inhibitor in the inhibition of eIF4E/eIF4G interaction, thus preventing the eIF4F complex for

116 d eIF4G binding, 4EGI-1, decreased the eIF4E/eIF4G expression and reduced the proliferation.

117 Here, we show that the eIF4E/eIF4G inhibitor 4EGI-1 acts allosterically by binding to

118 ion inhibitor 1 (4EGI-1), disrupts the eIF4E/eIF4G interaction and promotes binding of 4E-BP1 to eIF4

119 Thus, inhibiting the eIF4E/eIF4G interaction has emerged as a previously unpursued

120 ulation of the interaction between the eIF4E/eIF4G subunits of the translation initiation factor comp

121 ered small-molecule inhibitors of this eIF4E/eIF4G interaction (4EGIs) that inhibit translation initi

122 The eIF4E:eIF4G interaction was not inhibited but rather increased

123 mixed complexes (eIF4E-eIFiso4G or eIFiso4E-eIF4G) were expressed and purified from Escherichia coli

124 The elevated eIF4G in response to equol was not associated with eIF4E

125 4E counteracts this autoinhibition, enabling eIF4G to stimulate eIF4A helicase activity.

126 ecific to plants, is unique among eukaryotic eIF4G proteins in that it is highly divergent and unusua

127 The naturally evolved eIF4G gene expression noise minimum maps within the opti

128 th the general translation initiation factor eIF4G and promotes translation of a subset of these irre

129 tion factor eIF4E with the initiation factor eIF4G recruits the 40S ribosomal particle to the 5' end

130 and binding to translation initiation factor eIF4G to promote mRNA translation.

131 rotein and the translation initiation factor eIF4G.

132 nd cleaves the translation initiation factor eIF4G.

133 acts with host translation initiation factor eIF4G.

134 the kl-TSS by sequestering initiation factor eIF4G.

135 teraction with eukaryotic translation factor eIF4G, which then facilitates the assembly of the eIF4F

136 of the central domain of initiation factor, eIF4G to the J-K domains, which is stimulated by eIF4A.

137 , a homolog of canonical translation factor, eIF4G, which lacks PABP- and cap binding complex-interac

138 on complex formation coordinated by flexible eIF4G structure.

139 For eIF4G, all 2A(pro) proteases cleaved at similar sites, b

140 nslation and demonstrates novel activity for eIF4G in the regulation of translation.

141 kes up at least part of the binding site for eIF4G, we examined the effects of 3e5 expression on prot

142 rinting experiments revealed that functional eIF4G fragments protect the highly conserved stem-loop I

143 ctor 4 (eIF4)E, with activators (eIF4 gamma (eIF4G)) and inhibitors (eIF4E-binding protein 1 (4E-BP1)

144 anism for DEAD-box ATPase regulation by Gle1/eIF4G-like activators.

145 (5'-UTR) remains solvent-accessible at high eIF4G concentrations.

146 To determine how eIF4G recruits the mRNA, three eIF4G deletion mutants we

147 Similarly, a C-terminal fragment of human eIF4G-1, eIF4G(1357-1600), which prevents binding of MNK

148 We show that human eIF4G-like spliceosomal protein (h)CWC22 directly intera

149 ions between Ascaris eIF4E and the SL impact eIF4G and contribute to translation initiation, whereas

150 Engineered changes in eIF4G abundance amplify noise, demonstrating that minimu

151 screte approximately 90 amino acid domain in eIF4G is responsible for binding to eIF3, but the identi

152 (2020) report a neuron-specific microexon in eIF4G translation initiation factors that dampens synapt

153 Such regions are also present in eIF4G and have been reported to associate with mRNA bind

154 The region in eIF4G between the eIF4E-binding site and the MIF4G regio

155 stimulates PV-1(M) IRES activity by inducing eIF4G to bind in the optimal position and orientation to

156 omplex essential for translation initiation, eIF4G-eIF4A, and we demonstrate that Gle1(InsP6) and eIF

157 00), which prevents binding of MNK to intact eIF4G, reduces eIF4E phosphorylation and inhibits transl

158 sequence independently of eIF4E but involves eIF4G.

159 rly involves interaction with eIF4G, but its eIF4G-interacting domain is structurally distinct, altho

160 C-terminal domain (eIF5-CTD) directly links eIF4G to the preinitiation complex (PIC) and enhances mR

161 ificant down-regulation of eIF4GI (the major eIF4G isoform), as well as reduces levels of some, but n

162 Mammalian eIF4G contains three HEAT domains and unstructured regio

163 (Cucumis melo) eIF4E in complex with a melon eIF4G peptide and propose the first eIF4E-eIF4G structur

164 in vivo, identifying human NOM1 as a missing eIF4G-like interacting partner of eIF4AIII.

165 Thus, Mnk-eIF4G interaction is important for eIF4E phosphorylation

166 E phosphorylation through modulation of Mnk1-eIF4G interaction.

167 have overlapping functions in forming native eIF4G*mRNA*PABP complexes.

168 Nevertheless, eIF4G and eIFiso4G from wheat exhibit preferences in the

169 interactions of eIF4A with HEAT domain 2 of eIF4G and decreased association of eIF4G/-4A with RNA.

170 tween the average intracellular abundance of eIF4G and rates of cell population growth and global mRN

171 main 2 of eIF4G and decreased association of eIF4G/-4A with RNA.

172 ion factor 4E (eIF4E), preventing binding of eIF4G and the recruitment of the small ribosomal subunit

173 A comparison of the binding of eIF4G deletion mutants with BTEs containing mutations sh

174 regulates release of 4E-BP1, and binding of eIF4G, to many mTORC1 target mRNAs, including those need

175 (PCBP2), and starts with specific binding of eIF4G/eIF4A to d11.

176 instance, initiation starts with binding of eIF4G/eIF4A.

177 Cleavage of eIF4G at times after ribosome loading on templates occur

178 Finally, we show that cleavage of eIF4G by the poliovirus 2A protease generates a high-aff

179 ns attributed to 2A(pro) include cleavage of eIF4G-I and -II to inhibit cellular mRNA translation and

180 Using a series of deletion constructs of eIF4G, we demonstrate that its three previously elucidat

181 However, the proteolytic degradation of eIF4G alone by the human rhinovirus 2A protease abrogate

182 of eIF4E, eIF4G, and Pab1, and depletion of eIF4G mimics the translational defects of ASC1 mutants.

183 tion mechanism leading to the dislocation of eIF4G from eIF4E.

184 mRNP composition, marked by dissociation of eIF4G and PABP, and by recruitment of DDX6.

185 and show that the functional core domain of eIF4G plus an adjacent probable RNA-binding domain media

186 The HEAT domain of eIF4G stabilizes the active conformation of eIF4A requir

187 main DEAD-Box helicase, the HEAT-1 domain of eIF4G, and their complex.

188 ge of these IRESs from the central domain of eIF4G.

189 data suggest that the RNA binding domains of eIF4G provide the S. cerevisiae eIF4F complex with a sec

190 ntially depend on the stimulatory effects of eIF4G-dependent closed-loop assembly.

191 d 4E-BP2, suggesting that the interaction of eIF4G with eIF4E is controlled primarily through the 4E-

192 ncer cells, equol induced elevated levels of eIF4G, which were associated with increased cell viabili

193 the presence of the central domain (p50) of eIF4G, and p50 binding is likewise modified if PTB is pr

194 we also show that eIF4E promotes the rate of eIF4G cleavage by the 2A protease.

195 sites on the BTE and identified a region of eIF4G that is crucial for BTE binding.

196 interact directly with the middle region of eIF4G, however, we were unable to obtain any evidence fo

197 tly of eIF4A binding to the middle region of eIF4G.

198 Therefore, up-regulation of eIF4G by equol may result in increased translation of pr

199 at matches key eIF4A-interacting residues of eIF4G when superimposed on the X-ray structure of the eI

200 stem loop, very close to the binding site of eIF4G, and RBDs3 and 4 interact with the single-stranded

201 Plasmid-mediated synthesis of eIF4G imposes increased global gene expression stochasti

202 Targeting of eIF4G results in an impairment of 40S ribosome scanning

203 s a high-affinity IRES binding truncation of eIF4G that stimulates eIF4A duplex unwinding independent

204 complex with, and requires the activity of, eIF4G.

205 The IRES was dependent on eIF4G, but not eIF4E, for activity.

206 also suggest that the eIF4A-binding site on eIF4G made of the HEAT domain stimulates the ribosomal s

207 ated the interaction of eIF4E with 4E-BP1 or eIF4G during interphase and mitosis.

208 y, we show that eIFiso4G is similar to other eIF4G proteins in that there are interaction domains for

209 Assaying RNA-dependent PABP-eIF4G association in cell extracts suggests that RNA1, t

210 Surprisingly, ICP27-PABP-eIF4G complexes act independently of the effects of PABP

211 xes act independently of the effects of PABP-eIF4G on cap binding to promote small ribosomal subunit

212 Our findings indicate that PABP-eIF4G association is only one of several interactions th

213 onal activation and the function of the PABP-eIF4G complex in translation initiation.

214 oospermia-like (Dazl), also employs the PABP-eIF4G interaction in a similar manner.

215 e translation initiation as part of the PABP-eIF4G-eIF4E complex that stimulates the initial cap-bind

216 ize that closed-loop mRNP formation via PABP-eIF4G interaction is non-essential in vivo.

217 east eIF4G, the domain organization of plant eIF4G proteins is largely unknown.

218 tle is known about the conservation of plant eIF4G with those in other eukaryotes.

219 h functional analyses demonstrate that plant eIF4G binds to eIF4E through both the canonical and nonc

220 Interaction with the scaffolding protein eIF4G, which also binds eIF4E, brings Mnk and its substr

221 binding protein, and the scaffolding protein eIF4G.

222 simultaneously with the scaffolding protein eIF4G.

223 The accessory proteins eIF4G, eIF4B, and eIF4H enhance the duplex unwinding act

224 when complexed with two accessory proteins, eIF4G and eIF4B.

225 in human SCC cells (A431 and SCC-13) reduced eIF4G and proteins that regulate the cell cycle and prol

226 vitro, equol, but not daidzein, up-regulated eIF4G without affecting eIF4E or its regulator, 4E-bindi

227 the helicase eIF4A, and the central scaffold eIF4G, is a convergence node for a complex signaling net

228 Many eukaryotes express two highly similar eIF4G isoforms.

229 ents confirm the role of RNA1 in stabilizing eIF4G-mRNA association, and further indicate that RNA1 a

230 the concentration of eIF4F complex subunits eIF4G and eIF4E.

231 eIF4F is comprised of the subunits eIF4G and eIF4E and often the helicase, eIF4A.

232 escence anisotropy assay to demonstrate that eIF4G binds to eIF3 independently of eIF4A binding to th

233 tion through its RGG motif and indicate that eIF4G plays an important role as a scaffolding protein f

234 multiple cross-linker positions reveals that eIF4G contains two distinct eIF3-binding subdomains with

235 Here we show that eIF4G, the major scaffolding protein in the translation

236 m on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a sin

237 The eIF4G subunit serves as an assembly point for other init

238 ion and re-initiation also in yeast, and the eIF4G interaction with the mRNA-cap appears to promote e

239 at Scd6 represses translation by binding the eIF4G subunit of eIF4F in a manner dependent on its RGG

240 (BTE) stimulates translation by binding the eIF4G subunit of translation initiation factor eIF4F wit

241 Translation driven by the eIF4G-independent hepatitis C virus internal ribosome en

242 is the eIF4F cap recognition component, the eIF4G subunit associates with 40S-bound eIF3.

243 First, the eIF4G-RS1 interaction with the eIF5 C-terminal domain (e

244 was investigated using null mutants for the eIF4G isoforms in Arabidopsis.

245 binding to a site on eIF4E distant from the eIF4G binding epitope.

246 structural properties of the BTE, mapped the eIF4G-binding sites on the BTE and identified a region o

247 eases correlated fluctuations in part of the eIF4G binding site.

248 sed to examine functional differences of the eIF4G isoforms in Arabidopsis.

249 n of eIF4G1 that coordinates assembly of the eIF4G/-4A/-4B helicase complex and binding of the mitoge

250 ver, the individual domains of eIF4A, or the eIF4G-HEAT-1 domain alone show little structural changes

251 eIF4G isoforms that are highly similar, the eIF4G isoforms in plants, referred to as eIF4G and eIFis

252 In this study, the eIF4G isoform specificity of Omega was used to examine f

253 These results suggest that the eIF4G or eIFiso4G subunits influence translational effic

254 king approach, we unexpectedly show that the eIF4G-binding surface in eIF3 is comprised of the -c, -d

255 c activity, phenotypes not observed with the eIF4G loss of function mutant.

256 determine how eIF4G recruits the mRNA, three eIF4G deletion mutants were constructed: (i) eIF4G601-11

257 m7GTP cap-binding protein), whose binding to eIF4G (a scaffolding subunit) and eIF4A (an ATP-dependen

258 First, eIF4E binding to eIF4G generates a high-affinity binding conformation of

259 Second, eIF4E binding to eIF4G strongly stimulates the rate of duplex unwinding b

260 abundance by RNAi impaired eIF4E binding to eIF4G, thereby reducing assembly of the multisubunit ini

261 3e was sufficient to promote Mnk1-binding to eIF4G.

262 This liberates eIF4E and allows binding to eIF4G.

263 tion indicated diminished binding of eIF3 to eIF4G, signifying a reduction in recruitment of the mRNA

264 ses of mRNA translation: binding of eIF4A to eIF4G, reduction in PDCD4 expression and inhibition of i

265 requires concomitant association of eIF4E to eIF4G as well as S6K1 activity and that the persistence

266 IF4G(1357-1600) decrease binding of eIF4E to eIF4G.

267 nravel the effects of signal transduction to eIF4G on translation, we used specific activation of pro

268 eukaryotic initiation factor of translation eIF4G in cardiomyocytes, thereby counterbalancing the sh

269 Although many eukaryotes express two eIF4G isoforms that are highly similar, the eIF4G isofor

270 Plants, like many eukaryotes, express two eIF4G isoforms.

271 of tobacco mosaic virus preferentially uses eIF4G in wheat germ lysate.

272 rate preferences and cleavage kinetics using eIF4G from cellular extracts and Nups presented in nativ

273 minal region of VPg is important for the VPg-eIF4G interaction; viruses with mutations that alter or

274 tionship fits a computational model in which eIF4G is at the core of a multi-component-complex assemb

275 implicated in synaptic plasticity, and with eIF4G, a key regulator of translational initiation.

276 eIF4E with the m(7)GTP cap of mRNA and with eIF4G.

277 o eIF4E, thereby preventing association with eIF4G through an allosteric mechanism.

278 70) that control the exchange of 4E-BP1 with eIF4G at the 5' cap of CHK1 and other target mRNAs.

279 n by weakening their ability to compete with eIF4G for eIF4E binding within the translation initiatio

280 translation in eukaryotes by competing with eIF4G for an interaction with eIF4E.

281 t interaction of their eIF3 constituent with eIF4G.

282 l domain (NTD) with eIF4A, and Ded1-CTD with eIF4G, subunits of eIF4F, enhance Ded1 unwinding activit

283 s NTD with eIF4E and eIF4A, and its CTD with eIF4G.

284 lso found that the interaction of eIF4E with eIF4G was maintained in the liver of fasted rats as well

285 ranslation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation.

286 from eIF4E, allowing eIF4E to interact with eIF4G and translation initiation to resume.

287 ting kinases (Mnk), which also interact with eIF4G.

288 first functions by directly interacting with eIF4G to assemble a Ded1-mRNA-eIF4F complex, which accum

289 d that maintenance of eIF4E interaction with eIF4G was not by itself sufficient to sustain global rat

290 function similarly involves interaction with eIF4G, but its eIF4G-interacting domain is structurally

291 omain of Mnk1 restricts its interaction with eIF4G, preventing eIF4E phosphorylation in the absence o

292 that Mnk1 autoregulates its interaction with eIF4G, releasing itself from the scaffold after phosphor

293 etermined by their specific interaction with eIF4G.

294 ts consensus sequence YXXXXLPhi, shared with eIF4G, and is a nucleocytoplasmic shuttling protein foun

295 and exhibits more functional similarity with eIF4G than with eIFiso4G1 during Omega-mediated translat

296 and form functional complexes in vitro with eIF4G.

297 which indicates that eIF4A, with and without eIF4G, acts as a modulator for activity and substrate pr

298 Association of eIF4A with WT eIF4G in vivo also was enhanced by yeIF4B overexpression

299 Unlike animal and yeast eIF4G, the domain organization of plant eIF4G proteins i

300 g a conformation of the HEAT domain of yeast eIF4G conducive for stable binding to eIF4A.