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PDBsum entry 1ej4
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Translation PDB id
1ej4

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
179 a.a. *
14 a.a. *
Ligands
M7G
Waters ×85
* Residue conservation analysis
PDB id:
1ej4
Name: Translation
Title: Cocrystal structure of eif4e/4e-bp1 peptide
Structure: Eukaryotic initiation factor 4e. Chain: a. Fragment: residues 28-217. Engineered: yes. Eukaryotic translation initiation factor 4e binding protein 1. Chain: b. Fragment: residues 51-67. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this peptide was chemically synthesized. The sequence of this peptide naturally occurs in humans (homo sapiens)
Biol. unit: Tetramer (from PQS)
Resolution:
2.25Å     R-factor:   0.219     R-free:   0.267
Authors: J.Marcotrigiano,A.-C.Gingras,N.Sonenberg,S.K.Burley
Key ref:
J.Marcotrigiano et al. (1999). Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol Cell, 3, 707-716. PubMed id: 10394359 DOI: 10.1016/S1097-2765(01)80003-4
Date:
29-Feb-00     Release date:   15-Mar-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P63073  (IF4E_MOUSE) -  Eukaryotic translation initiation factor 4E from Mus musculus
Seq:
Struc: 		217 a.a.
179 a.a.
Protein chain
Pfam   ArchSchema ?
Q13541  (4EBP1_HUMAN) -  Eukaryotic translation initiation factor 4E-binding protein 1 from Homo sapiens
Seq:
Struc: 		118 a.a.
14 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/S1097-2765(01)80003-4 Mol Cell 3:707-716 (1999)
PubMed id: 10394359  
 
 
Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G.
J.Marcotrigiano, A.C.Gingras, N.Sonenberg, S.K.Burley.
 
  ABSTRACT  
 
eIF4G uses a conserved Tyr-X-X-X-X-Leu-phi segment (where X is variable and phi is hydrophobic) to recognize eIF4E during cap-dependent translation initiation in eukaryotes. High-resolution X-ray crystallography and complementary biophysical methods have revealed that this eIF4E recognition motif undergoes a disorder-to-order transition, adopting an L-shaped, extended chain/alpha-helical conformation when it interacts with a phylogenetically invariant portion of the convex surface of eIF4E. Inhibitors of translation initiation known as eIF4E-binding proteins (4E-BPs) contain similar eIF4E recognition motifs. These molecules are molecular mimics of eIF4G, which act by occupying the same binding site on the convex dorsum of eIF4E and blocking assembly of the translation machinery. The implications of our results for translation initiation are discussed in detail, and a molecular mechanism for relief of translation inhibition following phosphorylation of the 4E-BPs is proposed.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Structures of Two Murine eIF4E/7-methyl-GDP/Peptide Ternary ComplexesRibbon diagrams of the eIF4E (blue)/7-methyl-GDP (ball-and-stick representation)/peptide ternary complex structures viewed perpendicular to the eIF4E’s β sheet (A and C) and in profile, rotated 90° about the vertical from the previous view (B and D). 7-methyl-GDP is located in the cap-binding slot on the convex face of eIF4E, 35 Å from peptide binding site.Upper: The eIF4GII peptide (orange) forms an L-shaped structure that interacts with the N terminus of eIF4E and two of three long α helices (H1 and H2) on its convex dorsal surface.Lower: The 4E-BP1 peptide (yellow) adopts a very similar conformation on binding to eIF4E.
Figure 5.
Figure 5. eIF4GII and 4E-BP1 Peptides Binding to the Convex Dorsal Surface of eIF4EGRASP ([8]) representation of the eIF4E surface, colored coded for electrostatic potential (red < −10 kBT; blue > 10 kBT), calculated in the absence of the peptides (see Figure 5C in [21]) using a water probe radius of 1.4 Å. The (A) eIF4GII and (B) 4E-BP1 peptides are depicted with orange and yellow, respectively. (C) Overlay of the eIF4GII (orange) and 4E-BP1 (yellow) peptides with the solvent-accessible convex surface of eIF4E, colored green for residues that are absolutely conserved among all known eIF4E sequences ([21]).
 
  The above figures are reprinted by permission from Cell Press: Mol Cell (1999, 3, 707-716) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21283665 J.A.Ashby, C.E.Stevenson, G.E.Jarvis, D.M.Lawson, and A.J.Maule (2011).
Structure-Based Mutational Analysis of eIF4E in Relation to sbm1 Resistance to Pea Seed-Borne Mosaic Virus in Pea.
  PLoS One, 6, e15873.
PDB code: 2wmc
21183464 P.Gosselin, N.Oulhen, M.Jam, J.Ronzca, P.Cormier, M.Czjzek, and B.Cosson (2011).
The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.
  Nucleic Acids Res, 39, 3496-3503.  
19926289 G.Hernández, M.Altmann, and P.Lasko (2010).
Origins and evolution of the mechanisms regulating translation initiation in eukaryotes.
  Trends Biochem Sci, 35, 63-73.  
20528734 H.Zhou, and S.Huang (2010).
mTOR Signaling in cancer cell motility and tumor metastasis.
  Crit Rev Eukaryot Gene Expr, 20, 1.  
19741065 J.L.Gallois, C.Charron, F.Sánchez, G.Pagny, M.C.Houvenaghel, A.Moretti, F.Ponz, F.Revers, C.Caranta, and S.German-Retana (2010).
Single amino acid changes in the turnip mosaic virus viral genome-linked protein (VPg) confer virulence towards Arabidopsis thaliana mutants knocked out for eukaryotic initiation factors eIF(iso)4E and eIF(iso)4G.
  J Gen Virol, 91, 288-293.  
20965418 K.A.Spriggs, M.Bushell, and A.E.Willis (2010).
Translational regulation of gene expression during conditions of cell stress.
  Mol Cell, 40, 228-237.  
20347422 M.Bidinosti, I.Ran, M.R.Sanchez-Carbente, Y.Martineau, A.C.Gingras, C.Gkogkas, B.Raught, C.R.Bramham, W.S.Sossin, M.Costa-Mattioli, L.DesGroseillers, J.C.Lacaille, and N.Sonenberg (2010).
Postnatal deamidation of 4E-BP2 in brain enhances its association with raptor and alters kinetics of excitatory synaptic transmission.
  Mol Cell, 37, 797-808.  
20424163 M.Bidinosti, Y.Martineau, F.Frank, and N.Sonenberg (2010).
Repair of isoaspartate formation modulates the interaction of deamidated 4E-BP2 with mTORC1 in brain.
  J Biol Chem, 285, 19402-19408.  
20880835 S.Tait, K.Dutta, D.Cowburn, J.Warwicker, A.J.Doig, and J.E.McCarthy (2010).
Local control of a disorder-order transition in 4E-BP1 underpins regulation of translation via eIF4E.
  Proc Natl Acad Sci U S A, 107, 17627-17632.  
19114555 A.Yanagiya, Y.V.Svitkin, S.Shibata, S.Mikami, H.Imataka, and N.Sonenberg (2009).
Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap.
  Mol Cell Biol, 29, 1661-1669.  
21082945 K.Sankhala, and F.J.Giles (2009).
Potential of mTOR inhibitors as therapeutic agents in hematological malignancies.
  Expert Rev Hematol, 2, 399-414.  
19146809 M.Costa-Mattioli, W.S.Sossin, E.Klann, and N.Sonenberg (2009).
Translational control of long-lasting synaptic plasticity and memory.
  Neuron, 61, 10-26.  
  19297425 N.K.McGhee, L.S.Jefferson, and S.R.Kimball (2009).
Elevated corticosterone associated with food deprivation upregulates expression in rat skeletal muscle of the mTORC1 repressor, REDD1.
  J Nutr, 139, 828-834.  
19239892 N.Sonenberg, and A.G.Hinnebusch (2009).
Regulation of translation initiation in eukaryotes: mechanisms and biological targets.
  Cell, 136, 731-745.  
19237539 R.E.Rhoads (2009).
eIF4E: New Family Members, New Binding Partners, New Roles.
  J Biol Chem, 284, 16711-16715.  
19838324 R.S.Zukin, J.D.Richter, and C.Bagni (2009).
Signals, synapses, and synthesis: how new proteins control plasticity.
  Front Neural Circuits, 3, 14.  
  19641745 R.Tuteja (2009).
Identification and bioinformatics characterization of translation initiation complex eIF4F components and poly(A)-binding protein from Plasmodium falciparum.
  Commun Integr Biol, 2, 245-260.  
19268617 S.Iwasaki, T.Kawamata, and Y.Tomari (2009).
Drosophila argonaute1 and argonaute2 employ distinct mechanisms for translational repression.
  Mol Cell, 34, 58-67.  
19952439 T.Ishida (2009).
Structural studies of specific intermolecular interactions and self-aggregation of biomolecules and their application to drug design.
  Chem Pharm Bull (Tokyo), 57, 1309-1334.  
19710013 W.Liu, R.Zhao, C.McFarland, J.Kieft, A.Niedzwiecka, M.Jankowska-Anyszka, J.Stepinski, E.Darzynkiewicz, D.N.Jones, and R.E.Davis (2009).
Structural insights into parasite eIF4E binding specificity for m7G and m2,2,7G mRNA caps.
  J Biol Chem, 284, 31336-31349.
PDB codes: 3hxg 3hxi
19850929 Y.Suzuki, M.Minami, M.Suzuki, K.Abe, S.Zenno, M.Tsujimoto, K.Matsumoto, and Y.Minami (2009).
The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.
  J Biol Chem, 284, 35597-35604.  
19321500 Y.Yoffe, M.Léger, A.Zinoviev, J.Zuberek, E.Darzynkiewicz, G.Wagner, and M.Shapira (2009).
Evolutionary changes in the Leishmania eIF4F complex involve variations in the eIF4E-eIF4G interactions.
  Nucleic Acids Res, 37, 3243-3253.  
18250159 D.Walsh, C.Arias, C.Perez, D.Halladin, M.Escandon, T.Ueda, R.Watanabe-Fukunaga, R.Fukunaga, and I.Mohr (2008).
Eukaryotic translation initiation factor 4F architectural alterations accompany translation initiation factor redistribution in poxvirus-infected cells.
  Mol Cell Biol, 28, 2648-2658.  
18442140 H.Soma, I.Yabe, A.Takei, N.Fujiki, T.Yanagihara, and H.Sasaki (2008).
Associations between multiple system atrophy and polymorphisms of SLC1A4, SQSTM1, and EIF4EBP1 genes.
  Mov Disord, 23, 1161-1167.  
18805096 I.Napoli, V.Mercaldo, P.P.Boyl, B.Eleuteri, F.Zalfa, S.De Rubeis, D.Di Marino, E.Mohr, M.Massimi, M.Falconi, W.Witke, M.Costa-Mattioli, N.Sonenberg, T.Achsel, and C.Bagni (2008).
The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP.
  Cell, 134, 1042-1054.  
17667941 J.W.Shih, T.Y.Tsai, C.H.Chao, and Y.H.Wu Lee (2008).
Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein.
  Oncogene, 27, 700-714.  
18480444 S.German-Retana, J.Walter, B.Doublet, G.Roudet-Tavert, V.Nicaise, C.Lecampion, M.C.Houvenaghel, C.Robaglia, T.Michon, and O.Le Gall (2008).
Mutational analysis of plant cap-binding protein eIF4E reveals key amino acids involved in biochemical functions and potyvirus infection.
  J Virol, 82, 7601-7612.  
18614538 S.V.Slepenkov, N.L.Korneeva, and R.E.Rhoads (2008).
Kinetic mechanism for assembly of the m7GpppG.eIF4E.eIF4G complex.
  J Biol Chem, 283, 25227-25237.  
18651095 X.H.Liao, A.Majithia, X.Huang, and A.R.Kimmel (2008).
Growth control via TOR kinase signaling, an intracellular sensor of amino acid and energy availability, with crosstalk potential to proline metabolism.
  Amino Acids, 35, 761-770.  
17254965 N.J.Moerke, H.Aktas, H.Chen, S.Cantel, M.Y.Reibarkh, A.Fahmy, J.D.Gross, A.Degterev, J.Yuan, M.Chorev, J.A.Halperin, and G.Wagner (2007).
Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G.
  Cell, 128, 257-267.  
17942399 N.Minshall, M.H.Reiter, D.Weil, and N.Standart (2007).
CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes.
  J Biol Chem, 282, 37389-37401.  
18082597 N.Sonenberg, and A.G.Hinnebusch (2007).
New modes of translational control in development, behavior, and disease.
  Mol Cell, 28, 721-729.  
18302007 R.M.Bannen, C.A.Bingman, and G.N.Phillips (2007).
Effect of low-complexity regions on protein structure determination.
  J Struct Funct Genomics, 8, 217-226.  
17352659 Y.F.Chang, J.S.Imam, and M.F.Wilkinson (2007).
The nonsense-mediated decay RNA surveillance pathway.
  Annu Rev Biochem, 76, 51-74.  
16766523 A.K.LeFebvre, N.L.Korneeva, M.Trutschl, U.Cvek, R.D.Duzan, C.A.Bradley, J.W.Hershey, and R.E.Rhoads (2006).
Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit.
  J Biol Chem, 281, 22917-22932.  
16481474 D.Walsh, and I.Mohr (2006).
Assembly of an active translation initiation factor complex by a viral protein.
  Genes Dev, 20, 461-472.  
16305812 I.Mohr (2006).
Phosphorylation and dephosphorylation events that regulate viral mRNA translation.
  Virus Res, 119, 89-99.  
16698552 L.Bellsolell, P.F.Cho-Park, F.Poulin, N.Sonenberg, and S.K.Burley (2006).
Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1.
  Structure, 14, 913-923.  
17036047 L.Volpon, M.J.Osborne, I.Topisirovic, N.Siddiqui, and K.L.Borden (2006).
Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands.
  EMBO J, 25, 5138-5149.
PDB code: 2gpq
16705177 M.Y.Jung, L.Lorenz, and J.D.Richter (2006).
Translational control by neuroguidin, a eukaryotic initiation factor 4E and CPEB binding protein.
  Mol Cell Biol, 26, 4277-4287.  
16303201 R.E.Lloyd (2006).
Translational control by viral proteinases.
  Virus Res, 119, 76-88.  
16519694 T.Michon, Y.Estevez, J.Walter, S.German-Retana, and O.Le Gall (2006).
The potyviral virus genome-linked protein VPg forms a ternary complex with the eukaryotic initiation factors eIF4E and eIF4G and reduces eIF4E affinity for a mRNA cap analogue.
  FEBS J, 273, 1312-1322.  
17041626 Y.Mamane, E.Petroulakis, O.LeBacquer, and N.Sonenberg (2006).
mTOR, translation initiation and cancer.
  Oncogene, 25, 6416-6422.  
16191198 B.Joshi, K.Lee, D.L.Maeder, and R.Jagus (2005).
Phylogenetic analysis of eIF4E-family members.
  BMC Evol Biol, 5, 48.  
15897901 C.Constantinou, and M.J.Clemens (2005).
Regulation of the phosphorylation and integrity of protein synthesis initiation factor eIF4GI and the translational repressor 4E-BP1 by p53.
  Oncogene, 24, 4839-4850.  
15956551 D.Walsh, C.Perez, J.Notary, and I.Mohr (2005).
Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells.
  J Virol, 79, 8057-8064.  
  16511166 E.Bitto, C.A.Bingman, H.Robinson, S.T.Allard, G.E.Wesenberg, and G.N.Phillips (2005).
The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 812-817.
PDB code: 1ztp
16299530 I.Mohr (2005).
To replicate or not to replicate: achieving selective oncolytic virus replication in cancer cells through translational control.
  Oncogene, 24, 7697-7709.  
16046624 J.M.Bourhis, V.Receveur-Bréchot, M.Oglesbee, X.Zhang, M.Buccellato, H.Darbon, B.Canard, S.Finet, and S.Longhi (2005).
The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.
  Protein Sci, 14, 1975-1992.  
16314302 J.Magee, and J.Warwicker (2005).
Simulation of non-specific protein-mRNA interactions.
  Nucleic Acids Res, 33, 6694-6699.  
15611299 K.Mochizuki, A.Oguro, T.Ohtsu, N.Sonenberg, and Y.Nakamura (2005).
High affinity RNA for mammalian initiation factor 4E interferes with mRNA-cap binding and inhibits translation.
  RNA, 11, 77-89.  
15879529 L.Li, and C.C.Wang (2005).
Identification in the ancient protist Giardia lamblia of two eukaryotic translation initiation factor 4E homologues with distinctive functions.
  Eukaryot Cell, 4, 948-959.  
16186820 N.Hosoda, Y.K.Kim, F.Lejeune, and L.E.Maquat (2005).
CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells.
  Nat Struct Mol Biol, 12, 893-901.  
15882623 P.F.Cho, F.Poulin, Y.A.Cho-Park, I.B.Cho-Park, J.D.Chicoine, P.Lasko, and N.Sonenberg (2005).
A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP.
  Cell, 121, 411-423.  
15923620 R.Karni, Y.Gus, Y.Dor, O.Meyuhas, and A.Levitzki (2005).
Active Src elevates the expression of beta-catenin by enhancement of cap-dependent translation.
  Mol Cell Biol, 25, 5031-5039.  
15900314 S.J.Morley, M.J.Coldwell, and M.J.Clemens (2005).
Initiation factor modifications in the preapoptotic phase.
  Cell Death Differ, 12, 571-584.  
15971038 S.Ruffel, J.L.Gallois, M.L.Lesage, and C.Caranta (2005).
The recessive potyvirus resistance gene pot-1 is the tomato orthologue of the pepper pvr2-eIF4E gene.
  Mol Genet Genomics, 274, 346-353.  
15601834 T.D.Dinkova, B.D.Keiper, N.L.Korneeva, E.J.Aamodt, and R.E.Rhoads (2005).
Translation of a small subset of Caenorhabditis elegans mRNAs is dependent on a specific eukaryotic translation initiation factor 4E isoform.
  Mol Cell Biol, 25, 100-113.  
16287867 Y.V.Svitkin, B.Herdy, M.Costa-Mattioli, A.C.Gingras, B.Raught, and N.Sonenberg (2005).
Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation.
  Mol Cell Biol, 25, 10556-10565.  
15153109 B.Joshi, A.Cameron, and R.Jagus (2004).
Characterization of mammalian eIF4E-family members.
  Eur J Biochem, 271, 2189-2203.  
15209374 C.J.Richardson, S.S.Schalm, and J.Blenis (2004).
PI3-kinase and TOR: PIKTORing cell growth.
  Semin Cell Dev Biol, 15, 147-159.  
15075293 D.Walsh, and I.Mohr (2004).
Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells.
  Genes Dev, 18, 660-672.  
15070431 G.Sunavala-Dossabhoy, M.Fowler, and A.De Benedetti (2004).
Translation of the radioresistance kinase TLK1B is induced by gamma-irradiation through activation of mTOR and phosphorylation of 4E-BP1.
  BMC Mol Biol, 5, 1.  
15317596 J.L.Cowan, and S.J.Morley (2004).
The proteasome inhibitor, MG132, promotes the reprogramming of translation in C2C12 myoblasts and facilitates the association of hsp25 with the eIF4F complex.
  Eur J Biochem, 271, 3596-3611.  
14701818 J.Robalino, B.Joshi, S.C.Fahrenkrug, and R.Jagus (2004).
Two zebrafish eIF4E family members are differentially expressed and functionally divergent.
  J Biol Chem, 279, 10532-10541.  
15189156 L.D.Kapp, and J.R.Lorsch (2004).
The molecular mechanics of eukaryotic translation.
  Annu Rev Biochem, 73, 657-704.  
14685270 M.R.Nelson, A.M.Leidal, and C.A.Smibert (2004).
Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression.
  EMBO J, 23, 150-159.  
15062123 P.M.Macdonald (2004).
Translational control: a cup half full.
  Curr Biol, 14, R282-R283.  
15292274 S.Naegele, and S.J.Morley (2004).
Molecular cross-talk between MEK1/2 and mTOR signaling during recovery of 293 cells from hypertonic stress.
  J Biol Chem, 279, 46023-46034.  
15059963 S.Y.Chiu, F.Lejeune, A.C.Ranganathan, and L.E.Maquat (2004).
The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex.
  Genes Dev, 18, 745-754.  
15164008 T.von der Haar, J.D.Gross, G.Wagner, and J.E.McCarthy (2004).
The mRNA cap-binding protein eIF4E in post-transcriptional gene expression.
  Nat Struct Mol Biol, 11, 503-511.  
14557257 F.Poulin, A.Brueschke, and N.Sonenberg (2003).
Gene fusion and overlapping reading frames in the mammalian genes for 4E-BP3 and MASK.
  J Biol Chem, 278, 52290-52297.  
14675538 J.D.Gross, N.J.Moerke, T.von der Haar, A.A.Lugovskoy, A.B.Sachs, J.E.McCarthy, and G.Wagner (2003).
Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E.
  Cell, 115, 739-750.
PDB code: 1rf8
14645523 M.Miron, P.Lasko, and N.Sonenberg (2003).
Signaling from Akt to FRAP/TOR targets both 4E-BP and S6K in Drosophila melanogaster.
  Mol Cell Biol, 23, 9117-9126.  
12791690 N.Foeger, E.M.Schmid, and T.Skern (2003).
Human rhinovirus 2 2Apro recognition of eukaryotic initiation factor 4GI. Involvement of an exosite.
  J Biol Chem, 278, 33200-33207.  
12581660 N.Sonenberg, and T.E.Dever (2003).
Eukaryotic translation initiation factors and regulators.
  Curr Opin Struct Biol, 13, 56-63.  
14635255 T.Preiss, and M.W Hentze (2003).
Starting the protein synthesis machine: eukaryotic translation initiation.
  Bioessays, 25, 1201-1211.  
14675529 T.V.Pestova, and C.U.Hellen (2003).
Coupled folding during translation initiation.
  Cell, 115, 650-652.  
12368268 D.Niessing, S.Blanke, and H.Jäckle (2002).
Bicoid associates with the 5'-cap-bound complex of caudal mRNA and represses translation.
  Genes Dev, 16, 2576-2582.  
11875511 G.Varani, and F.H.Allain (2002).
How a rotavirus hijacks the human protein synthesis machinery.
  Nat Struct Biol, 9, 158-160.  
12086604 I.Groisman, M.Y.Jung, M.Sarkissian, Q.Cao, and J.D.Richter (2002).
Translational control of the embryonic cell cycle.
  Cell, 109, 473-483.  
12228254 N.Foeger, W.Glaser, and T.Skern (2002).
Recognition of eukaryotic initiation factor 4G isoforms by picornaviral proteinases.
  J Biol Chem, 277, 44300-44309.  
11836384 N.M.Kuyumcu-Martinez, M.Joachims, and R.E.Lloyd (2002).
Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease.
  J Virol, 76, 2062-2074.  
12110596 Q.Cao, and J.D.Richter (2002).
Dissolution of the maskin-eIF4E complex by cytoplasmic polyadenylation and poly(A)-binding protein controls cyclin B1 mRNA translation and oocyte maturation.
  EMBO J, 21, 3852-3862.  
12138083 S.J.Morley, and S.Naegele (2002).
Phosphorylation of eukaryotic initiation factor (eIF) 4E is not required for de novo protein synthesis following recovery from hypertonic stress in human kidney cells.
  J Biol Chem, 277, 32855-32859.  
11909525 T.E.Dever (2002).
Gene-specific regulation by general translation factors.
  Cell, 108, 545-556.  
11799119 T.P.Herbert, A.R.Tee, and C.G.Proud (2002).
The extracellular signal-regulated kinase pathway regulates the phosphorylation of 4E-BP1 at multiple sites.
  J Biol Chem, 277, 11591-11596.  
  11691836 A.C.Gingras, B.Raught, S.P.Gygi, A.Niedzwiecka, M.Miron, S.K.Burley, R.D.Polakiewicz, A.Wyslouch-Cieszynska, R.Aebersold, and N.Sonenberg (2001).
Hierarchical phosphorylation of the translation inhibitor 4E-BP1.
  Genes Dev, 15, 2852-2864.  
11416184 B.Raught, A.C.Gingras, and N.Sonenberg (2001).
The target of rapamycin (TOR) proteins.
  Proc Natl Acad Sci U S A, 98, 7037-7044.  
11214172 E.De Gregorio, J.Baron, T.Preiss, and M.W.Hentze (2001).
Tethered-function analysis reveals that elF4E can recruit ribosomes independent of its binding to the cap structure.
  RNA, 7, 106-113.  
11296278 G.Varani (2001).
Delivering messages from the 3' end.
  Proc Natl Acad Sci U S A, 98, 4288-4289.  
11483729 I.K.Ali, L.McKendrick, S.J.Morley, and R.J.Jackson (2001).
Activity of the hepatitis A virus IRES requires association between the cap-binding translation initiation factor (eIF4E) and eIF4G.
  J Virol, 75, 7854-7863.  
11172724 J.Marcotrigiano, I.B.Lomakin, N.Sonenberg, T.V.Pestova, C.U.Hellen, and S.K.Burley (2001).
A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery.
  Mol Cell, 7, 193-203.
PDB code: 1hu3
11461703 K.Kamada, F.Shu, H.Chen, S.Malik, G.Stelzer, R.G.Roeder, M.Meisterernst, and S.K.Burley (2001).
Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.
  Cell, 106, 71-81.
PDB code: 1jfi
12067482 M.J.Clemens (2001).
Translational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins.
  J Cell Mol Med, 5, 221-239.  
11713305 M.Ptushkina, K.Berthelot, T.von der Haar, L.Geffers, J.Warwicker, and J.E.McCarthy (2001).
A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties.
  Nucleic Acids Res, 29, 4561-4569.  
11511540 S.Pyronnet, J.Dostie, and N.Sonenberg (2001).
Suppression of cap-dependent translation in mitosis.
  Genes Dev, 15, 2083-2093.  
11605658 X.Shen, K.Tomoo, S.Uchiyama, Y.Kobayashi, and T.Ishida (2001).
Structural and thermodynamic behavior of eukaryotic initiation factor 4E in supramolecular formation with 4E-binding protein 1 and mRNA cap analogue, studied by spectroscopic methods.
  Chem Pharm Bull (Tokyo), 49, 1299-1303.  
11551508 Y.Ishigaki, X.Li, G.Serin, and L.E.Maquat (2001).
Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20.
  Cell, 106, 607-617.  
10698948 E.Dehlin, M.Wormington, C.G.Körner, and E.Wahle (2000).
Cap-dependent deadenylation of mRNA.
  EMBO J, 19, 1079-1086.  
10913184 I.B.Lomakin, C.U.Hellen, and T.V.Pestova (2000).
Physical association of eukaryotic initiation factor 4G (eIF4G) with eIF4A strongly enhances binding of eIF4G to the internal ribosomal entry site of encephalomyocarditis virus and is required for internal initiation of translation.
  Mol Cell Biol, 20, 6019-6029.  
10856257 J.Dostie, M.Ferraiuolo, A.Pause, S.A.Adam, and N.Sonenberg (2000).
A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E.
  EMBO J, 19, 3142-3156.  
10958635 L.Aravind, and E.V.Koonin (2000).
Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.
  Genome Res, 10, 1172-1184.  
10845104 M.Pohl, R.O.Stuart, H.Sakurai, and S.K.Nigam (2000).
Branching morphogenesis during kidney development.
  Annu Rev Physiol, 62, 595-620.  
10882097 S.Pyronnet, L.Pradayrol, and N.Sonenberg (2000).
A cell cycle-dependent internal ribosome entry site.
  Mol Cell, 5, 607-616.  
10753934 T.P.Herbert, G.R.Kilhams, I.H.Batty, and C.G.Proud (2000).
Distinct signalling pathways mediate insulin and phorbol ester-stimulated eukaryotic initiation factor 4F assembly and protein synthesis in HEK 293 cells.
  J Biol Chem, 275, 11249-11256.  
10872469 A.C.Gingras, B.Raught, and N.Sonenberg (1999).
eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation.
  Annu Rev Biochem, 68, 913-963.  
10635326 B.Stebbins-Boaz, Q.Cao, C.H.de Moor, R.Mendez, and J.D.Richter (1999).
Maskin is a CPEB-associated factor that transiently interacts with elF-4E.
  Mol Cell, 4, 1017-1027.  
10500305 T.E.Dever (1999).
Translation initiation: adept at adapting.
  Trends Biochem Sci, 24, 398-403.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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