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 promotes recruitment of eIF4A to type 1 IRESs, and

6 eIF4G/eIF4A then restructure the region of ribosomal att

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

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

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

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

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

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

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

14 Eukaryotic translation initiation factor 4G (eIF4G) functions to organize the assembly of initiation

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

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

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

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

19 on initiation apparatus and ribosome adaptor eIF4G.

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

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

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

23 as reported previously in the absence of an eIF4G-derived peptide.

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

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

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

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

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

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

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 eIF4E and the interaction between eIF4E and eIF4G.

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

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

38 ith eIF3a and associates with the eIF4E- and eIF4G-containing m7G cap-binding complex.

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

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

45 ering with the interaction between Pab1p and eIF4G.

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

47 7-methylguanosine cap of messenger RNA, and eIF4G, which serves as a scaffold to recruit other trans

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

49 finity interaction occurring between VPg and eIF4G.

50 n number and organization to those of animal eIF4G.

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

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

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

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

55 role in stabilizing the interaction between eIF4G and eIF3.

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

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

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

59 The ability of mutant type 1 IRESs to bind eIF4G/eIF4A correlated with their translational activity

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

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

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

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

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

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

66 xes and that this interaction is mediated by eIF4G.

67 posed of eIF4E, which binds to the mRNA cap, eIF4G, which indirectly links the mRNA cap with the 43S

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

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

70 phorylation of the Mnk1 active site controls eIF4G binding.

71 Despite detailed eIF4G structure data, the mechanisms controlling initiat

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

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

74 nhibits translation initiation by displacing eIF4G and RNA from eIF4A.

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 as well as other initiation factors (eIF4A, eIF4G, PABP, and eIF3).

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

84 chinery through its interactions with eIF4A, eIF4G, eIF3, the poly(A)-binding protein (PABP), and RNA

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

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

87 eIF4A/eIF4G stimulated initiation only at low temperatures or

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

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

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

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

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

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

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

95 mRNA cap and poly(A) tail, as well as eIF4E, eIF4G, Pab1 and eIF3, and is dependent on the length of

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

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

98 not phosphorylate eIF1, eIF1A, eIF4A, eIF4E, eIF4G, eIFiso4E, or eIFiso4G.

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

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

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

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

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

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

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

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

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

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

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

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

111 te that the formation of the m(7)GpppG.eIF4E.eIF4G(557-646) complex obeys a sequential, random kineti

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

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

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

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

116 4EGI-1 is the prototypic inhibitor of eIF4E/eIF4G interaction, a potent inhibitor of translation ini

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

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

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

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

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

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

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 al GAIT complex that binds initiation factor eIF4G and represses translation.

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

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

132 rotein and the translation initiation factor eIF4G.

133 nd cleaves the translation initiation factor eIF4G.

134 acts with host translation initiation factor eIF4G.

135 the kl-TSS by sequestering initiation factor eIF4G.

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

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

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

139 on complex formation coordinated by flexible eIF4G structure.

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

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

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

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

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

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

157 sequence independently of eIF4E but involves eIF4G.

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

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

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

161 Mammalian eIF4G contains three HEAT domains and unstructured regio

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

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

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

165 E phosphorylation through modulation of Mnk1-eIF4G interaction.

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

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

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

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

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

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

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

173 IRESs, in which the key event is binding of eIF4G to the J-K domain adjacent to the Yn-Xm-AUG motif,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

188 fically interacts with 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 Evidence of eIF4G and Pab1 interaction supports the notion of a clos

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

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

194 The position and orientation of eIF4G relative to the Yn-Xm-AUG motif is analogous in ty

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

196 ding to m(7)GTP-Sepharose in the presence of eIF4G(557-646), but only with recombinant eIF4E that was

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

222 binding protein, and the scaffolding protein eIF4G.

223 simultaneously with the scaffolding protein eIF4G.

224 helicase and requires the accessory proteins eIF4G and eIF4H.

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

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

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

228 omes onto capped mRNA functionally replacing eIF4G.

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

230 Many eukaryotes express two highly similar eIF4G isoforms.

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

232 the concentration of eIF4F complex subunits eIF4G and eIF4E.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

257 that the PDCD4 MA3 domains compete with the eIF4G MA3 domain and RNA for eIF4A binding.

258 Thus, even though eIF4G(557-646) binds eIF4E tightly, it does not increase

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

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

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

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

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

264 3e was sufficient to promote Mnk1-binding to eIF4G.

265 This liberates eIF4E and allows binding to eIF4G.

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

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

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

269 inetic constants for the binding of eIF4E to eIF4G(557-646), both in the presence and absence of m(7)

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

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

272 ment of eIF4A to type 1 IRESs, and together, eIF4G and eIF4A induce conformational changes at their 3

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

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

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

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

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

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

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

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

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

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

283 t interaction of their eIF3 constituent 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.