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EIF4B (eukaryotic translation initiation factor 4B)

Written2014-04Thomas Sbarrato, Emilie Horvilleur, Tuija Pöyry, Anne E Willis
Medical Research Council Toxicology Unit, Hodgkin Building, PO Box 138, Lancaster Rd, Leicester, LE1 9HN, UK

Abstract Review on eIF4B, with data on DNA/RNA, on the protein encoded and where the gene is implicated.

(Note : for Links provided by Atlas : click)


Alias (NCBI)EIF-4B
LocusID (NCBI) 1975
Atlas_Id 53571
Location 12q13.13  [Link to chromosome band 12q13]
Location_base_pair Starts at 53006456 and ends at 53042215 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping EIF4B.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
EIF4B (12q13.13)::C3orf58 (3q24)EIF4B (12q13.13)::TNNC1 (3p21.1)EIF4B (12q13.13)::UPP1 (7p12.3)
FYTTD1 (3q29)::EIF4B (12q13.13)ZNF384 (12p13.31)::EIF4B (12q13.13)


  Figure 1: Schematic representation of eIF4B gene, which is composed of 15 exons shown in blue.
Description The eIF4B gene codes for EIF4B protein. eIF4B gene is 69.15 kb in length and is composed of 15 exons (Figure 1).
Transcription eIF4B mRNA is ubiquitously expressed, however, regulation of eIF4B transcription has not been studied in detail.


  Figure 2: Schematic representation of eIF4B protein. The numbers refer to amino acids flanking the functional domains. Ser406 and Ser422 that can be phosphorylated by several kinases are indicated.
Description eIF4B is a 79kDA protein composed of 611 residues. Many sites of phosphorylation have been found for this protein using proteomics tools, including 29 Ser, 13 Thr and 1 Tyr (Prasad et al., 2009). Among them, two have been validated by further studies. The best studied phosphorylation site is Ser422 by p70/S6kinase in response to mTOR pathway (Holz et al., 2005). Ser422 can also be phosphorylated by p90 (RSK) and PKB (Shahbazian et al., 2006; van Gorp et al., 2009). Ser406 phosphorylation is cell cycle dependent and under control of mTOR and MAP kinase pathways (van Gorp et al., 2009). Ser406 is a target of Pim kinases (Yang et al., 2013). Finally, eIF4B is cleaved by caspase 3 after Asp45 during apoptosis (Bushell et al., 2001) (Figure 2).
Expression The protein is reported to be expressed in most tissues, excluding liver, smooth muscle or soft tissues (Uhlen et al., 2010). Given the crucial role played by this protein in the cell, it is expected to be expressed ubiquitously albeit probably to different levels throughout different tissues.
Localisation eIF4B has a cytoplasmic localisation.
  Figure 3: Initiation of translation.
Function eIF4B is an RNA binding protein involved in the regulation of the initiation stage of protein synthesis. This protein is critical for the recruitment of the mRNA to the ribosome. It helps unwind secondary structures in the mRNA to allow ribosome scanning, via enhancing both ATPase and helicase activities of eIF4A.
Translation of an mRNA initiates with the binding of eukaryotic initiation factor complex eIF4F comprised of eIF4E, eIF4G and eIF4A (Pestova and Kolupaeva, 2002) (Figure 3):
- eIF4E interacts directly with the cap of the mRNA and helps recruit the machinery to the 5'end of the mRNA.
- eIF4G protein provides a scaffold, bridging interactions between eIF4A, eIF4E, eIF3, PABP and RNA.
- Secondary structures in the mRNA that can be detrimental to the binding/scanning of the ribosome are unwound by the helicase eIF4A and its cofactors eIF4B and eIF4H (Grifo et al., 1983; Lawson et al., 1989; Rozen et al., 1990).
The binding of this eIF4F complex allows for the circularisation of the mRNA and the subsequent recruitment of the 43S pre-initiation complex (PIC) composed of the small ribosomal subunit (40S), the ternary complex (eIF2/met-tRNA/GTP) and several initiation factors (eIF1, eIF1A, eIF3 and eIF5) (Deo et al., 1999; Imataka et al., 1998; Lamphear et al., 1995; Wells et al., 1998). This complex will then scan the untranslated region (UTR) of the mRNA until a start codon is recognised (Kozak, 2002).
eIF4B acts at different levels to stimulate translation initiation: 1) by enhancing the ATPase and helicase activities of eIF4A and 2) by facilitating the recruitment of the 43S PIC.

1) Role of eIF4B in the stimulation of eIF4A
Although the precise mechanisms of action of eIF4B on the enhanced helicase activity of eIF4F are not fully understood, knockdown/aberrant expression of eIF4B in mammalian cells led to the reduction/stimulation in translation of mRNAs containing highly structured 5'UTRs (Horvilleur et al., 2013; Shahbazian et al., 2010). Additionally, the ATPase and helicase activity of free eIF4A was shown to be significantly slower than the rates of translation initiation or the rates of scanning of the PIC (Grifo et al., 1984; Pause et al., 1994; Richter-Cook et al., 1998).
Consequently, one can envisage that eIF4B can help in the substrate (ATP and RNA) recognition by eIF4A. As such, eIF4B can modulate the affinity for ATP and RNA by inducing conformational changes in eIF4A (Bi et al., 2000; Marintchev et al., 2009; Methot et al., 1994; Nielsen et al., 2011; Rogers Jr. et al., 2001; Rozovsky et al., 2008). Additionally, eIF4B can enhance the efficiency of this process by coupling the ATP hydrolysis to duplex unwinding to avoid redundant, energy-consuming events (Ozes et al., 2011). In a manner similar to other single-stranded DNA binding proteins that associate with helicases, one possible mode of action for eIF4B is to stabilize newly unwound single-stranded RNA. In support of this, a direct interaction between eIF4A and eIF4B in the presence of RNA and an ATP analog have been established via the C terminal region of eIF4B (Nielsen et al., 2011; Rozovsky et al., 2008).

2) Role of eIF4B in the recruitment of 43S PIC to mRNAs
Through its various domains, eIF4B is now known to promote the association of the various players in the recruitment of the 43S PIC to the mRNA. The C terminal RNA binding domain of eIF4B enables its binding to mRNA whereas the RRM motif triggers interaction with the rRNA from the 43S PIC (Methot et al., 1996a; Naranda et al., 1994). The latter is thought to anchor the helicase eIF4A to the scanning ribosome (Methot et al., 1996a). Importantly, mammalian eIF4B dimerises and binds to eIF3a via its DRYG repeats, thus providing a main link between the eIF4F-loaded mRNA and the 43S PIC (Methot et al., 1996b).
These results provide evidence that eIF4B participates in recruitment and assembly of the PIC on mRNAs. Critically, recent findings have now shown that interactions involving eIF4B via its different domains are essential for the effective assembly and efficient scanning of the 43S PIC. Yeast eIF4B together with eIF4F and eIF3 decreased the dependency on high concentrations of eIF4A for the rapid assembly and recruitment of the 43S PIC on endogenous short leader mRNAs (Mitchell et al., 2010; Walker et al., 2013), thus eIF4B can mediate an enhancing effect on the PIC recruitment to an mRNA.

The spatial positioning of eIF4B on the scanning ribosome is poorly understood. The helicase complex eIF4A/eIF4B could be located near the mRNA exit channel (i.e. 5'/behind the scanning PIC) or alternatively at the mRNA entry channel (i.e. 3'/in front of the scanning PIC) (Figure 4). To support the former hypothesis, a Brownian ratchet model was proposed in which eIF4F is located near the exit channel of the PIC (Spirin, 2009). In this model, eIF4A-unwound and eIF4B-captured single-stranded RNA would be scanned by diffusion by the PIC. Contradictory, new evidence have shown that yeast eIF4B mapped to the head of the PIC near the entry channel (Walker et al., 2013). In such a case, the eIF4F complex would be recruited to the cap and would be located at the forefront of the PIC, thus allowing efficient unwinding and scanning (Marintchev et al., 2009). New experimental approaches, including structures of the human ribosome associated with factors, should be able to shed some light on the matter in the future.

  Figure 4: Two possible models for eIF4B position in the initiation complex during scanning of 5'UTR.
Homology eIF4B is one of the least conserved initiation factors in terms of sequence homology (Cheng and Gallie, 2006), however, its function is conserved and eIF4B homologues can be found across all eukaryotic species. In addition to the human eIF4B, one of the most studied eIF4B homologs is the yeast protein, TIF3 (Altmann et al., 1993). eIF4H is a 23kDa paralog of eIF4B showing homology to the RRM RNA binding domain. eIF4H stimulates eIF4A helicase activity in a similar way to eIF4B.

Implicated in

Entity General role in cancer
Note eIF4B expression and phosphorylation are de-regulated in many cancers. In particular, Ser422 phosphorylation is at the crossroad of two major pathways in oncogenesis: MAP kinases and AKT/mTOR pathway (Shahbazian et al., 2006) (Figure 5). In response to these signalling pathways, eIF4B activates both global translation, driving faster proliferation, and overexpression of specific oncoproteins such as MYC or BCL2 (Shahbazian et al., 2010). Activation of eIF4B and subsequent c-MYC induction is involved in arsenic-induced transformation in mouse epithelial cells (Zhang et al., 2011). Moreover, binding of 14-3-3 sigma tumour suppressor to eIF4B in late mitosis regulates translation indicating direct involvement of eIF4B in regulation of cell cycle (Wilker et al., 2007). Finally, eIF4B is cleaved by a caspase dependent mechanism upon activation of tumour necrosis factor pathway, suggesting a role in preventing apoptosis (Jeffrey et al., 2002).
Figure 5: mTOR and MEK/ERK/MAP kinase pathways converge on eIF4B.
Entity Nasopharyngeal carcinoma (NPC)
Note Although not mutated, p53 is known to be up-regulated in NPC. In a proteomic study, eIF4B was shown to be down-regulated following p53 knockdown in a NPC cell line (Sun et al., 2007).
Entity T-cell lymphoblastic leukemia/lymphoma
Note eIF4B mRNA was found to be up-regulated in a genome wide study comparing mouse model of thymic tumours (lymphoblastic leukaemia precursor) to untransformed thymus (Lin and Aplan, 2007).
Entity Gastric cancer
Note A microarray study found eIF4B mRNA to be up-regulated in a panel of 22 patients after they became resistant to combined cisplatin and fludarabine treatment (Kim et al., 2011).
Entity Non-small cell lung cancer (NSCLC)
Note Chromosomal aberrations in 12q13 region are frequent in NSCLC, where there can be either loss of heterozygocity or amplification, sometimes coupled with unbalanced translocation. eIF4B expression is significantly higher in NSCLC tumours showing this kind of alteration (Liang et al., 2013). Synergistic effect of mTOR and MEK inhibitors in NSCLC cell lines is correlated with significant decrease in eIF4B phosphorylation (Zou et al., 2012).
Entity Oral squamous cell carcinoma
Note Activation of Laminin γ2 by eIF4B is found in pre-malignant oral dysplasia, where eIF4B is activated by ERK/MAP kinase pathway (Degen et al., 2012). Laminin γ2 levels remain high in oral squamous cell carcinoma, although eIF4B has not been studied in this context.
Entity Prostatic cancer
Note In Prostatic carcinoma, eIF4B phosphorylation by Pim2 leads to resistance to apoptosis (Ren et al., 2013).
Entity Lymphangioleiomyomatosis
Note eIF4B phosphorylation increased following activation of mTOR pathway in lymphangioleiomyomatosis (Gu et al., 2013).
Entity Diffuse large B-cell lymphoma (DLBCL)
Note eIF4B is up-regulated following activation of mTOR pathway in DLBCL and, in turn, activates translation of proteins involved in DNA repair and inhibition of apoptosis. Elevated eIF4B level was shown to be poor prognosis in DLBCL (Horvilleur et al., 2013).
Entity Various cancers
Note Finally, amplification, duplication and deletion of 12q13 have been described in different cancers including sarcoma, glioma, bladder carcinoma or anaplastic lymphoma without direct involvement of eIF4B.

To be noted

Doctors Thomas Sbarrato and Emilie Horvilleur contributed equally to this work.


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This paper should be referenced as such :
T Sbarrato, E Horvilleur, T Pöyry, AE Willis
EIF4B (eukaryotic translation initiation factor 4B)
Atlas Genet Cytogenet Oncol Haematol. 2015;19(1):4-10.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)EIF4B   3285
Atlas Explorer : (Salamanque)EIF4B
Entrez_Gene (NCBI)EIF4B    eukaryotic translation initiation factor 4B
AliasesEIF-4B; PRO1843
GeneCards (Weizmann)EIF4B
Ensembl hg19 (Hinxton)ENSG00000063046 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000063046 [Gene_View]  ENSG00000063046 [Sequence]  chr12:53006456-53042215 [Contig_View]  EIF4B [Vega]
ICGC DataPortalENSG00000063046
TCGA cBioPortalEIF4B
Genatlas (Paris)EIF4B
SOURCE (Princeton)EIF4B
Genetics Home Reference (NIH)EIF4B
Genomic and cartography
GoldenPath hg38 (UCSC)EIF4B  -     chr12:53006456-53042215 +  12q13.13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EIF4B  -     12q13.13   [Description]    (hg19-Feb_2009)
GoldenPathEIF4B - 12q13.13 [CytoView hg19]  EIF4B - 12q13.13 [CytoView hg38]
Genome Data Viewer NCBIEIF4B [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB076839 AK092188 AK222528 AK293731 AK299329
RefSeq transcript (Entrez)NM_001300821 NM_001330654 NM_001417 NM_018507
Consensus coding sequences : CCDS (NCBI)EIF4B
Gene ExpressionEIF4B [ NCBI-GEO ]   EIF4B [ EBI - ARRAY_EXPRESS ]   EIF4B [ SEEK ]   EIF4B [ MEM ]
Gene Expression Viewer (FireBrowse)EIF4B [ Firebrowse - Broad ]
GenevisibleExpression of EIF4B in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1975
GTEX Portal (Tissue expression)EIF4B
Human Protein AtlasENSG00000063046-EIF4B [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP23588   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP23588  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP23588
Domaine pattern : Prosite (Expaxy)RRM (PS50102)   
Domains : Interpro (EBI)EIF-4B    Nucleotide-bd_a/b_plait_sf    RBD_domain_sf    RRM_dom   
Domain families : Pfam (Sanger)RRM_1 (PF00076)   
Domain families : Pfam (NCBI)pfam00076   
Domain families : Smart (EMBL)RRM (SM00360)  
Conserved Domain (NCBI)EIF4B
PDB (RSDB)1WI8    2J76    6FEC   
PDB Europe1WI8    2J76    6FEC   
PDB (PDBSum)1WI8    2J76    6FEC   
PDB (IMB)1WI8    2J76    6FEC   
Structural Biology KnowledgeBase1WI8    2J76    6FEC   
SCOP (Structural Classification of Proteins)1WI8    2J76    6FEC   
CATH (Classification of proteins structures)1WI8    2J76    6FEC   
AlphaFold pdb e-kbP23588   
Human Protein Atlas [tissue]ENSG00000063046-EIF4B [tissue]
Protein Interaction databases
IntAct (EBI)P23588
Ontologies - Pathways
Ontology : AmiGOformation of translation preinitiation complex  RNA binding  translation initiation factor activity  protein binding  cytosol  cytosol  regulation of translational initiation  eukaryotic translation initiation factor 4F complex  RNA strand annealing activity  RNA strand-exchange activity  ribosomal small subunit binding  eukaryotic translation initiation factor 4F complex assembly  
Ontology : EGO-EBIformation of translation preinitiation complex  RNA binding  translation initiation factor activity  protein binding  cytosol  cytosol  regulation of translational initiation  eukaryotic translation initiation factor 4F complex  RNA strand annealing activity  RNA strand-exchange activity  ribosomal small subunit binding  eukaryotic translation initiation factor 4F complex assembly  
REACTOMEP23588 [protein]
REACTOME PathwaysR-HSA-72706 [pathway]   
NDEx NetworkEIF4B
Atlas of Cancer Signalling NetworkEIF4B
Wikipedia pathwaysEIF4B
Orthology - Evolution
GeneTree (enSembl)ENSG00000063046
Phylogenetic Trees/Animal Genes : TreeFamEIF4B
Homologs : HomoloGeneEIF4B
Homology/Alignments : Family Browser (UCSC)EIF4B
Gene fusions - Rearrangements
Fusion : FusionHubAD_1--EIF4B    EEF1A1--EIF4B    EIF4B--ACOT9    EIF4B--ALB    EIF4B--ANK2    EIF4B--C3ORF58    EIF4B--CANX    EIF4B--CNOT10    EIF4B--DEK    EIF4B--EEF2   
EIF4B--EIF4BP7    EIF4B--GABBR2    EIF4B--GPSM3    EIF4B--GTPBP6    EIF4B--IFI16    EIF4B--ILF3    EIF4B--ITGA7    EIF4B--KCTD20    EIF4B--MACF1    EIF4B--MAF   
EIF4B--VTA1    EIF4B--WSB1    EIF4B--YY1    EIF4B--ZNF384    ERGIC3--EIF4B    FYTTD1--EIF4B    JA040725--EIF4B    NCAPD2--EIF4B    NUSAP1--EIF4B    PDLIM7--EIF4B   
PLOD1--EIF4B    SFSWAP--EIF4B    TLE3--EIF4B    TMTC3--EIF4B    ZNF384--EIF4B   
Fusion : QuiverEIF4B
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEIF4B [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EIF4B
Exome Variant ServerEIF4B
GNOMAD BrowserENSG00000063046
Varsome BrowserEIF4B
ACMGEIF4B variants
Genomic Variants (DGV)EIF4B [DGVbeta]
DECIPHEREIF4B [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEIF4B 
ICGC Data PortalEIF4B 
TCGA Data PortalEIF4B 
Broad Tumor PortalEIF4B
OASIS PortalEIF4B [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEIF4B  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEIF4B
Mutations and Diseases : HGMDEIF4B
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)EIF4B
DoCM (Curated mutations)EIF4B
CIViC (Clinical Interpretations of Variants in Cancer)EIF4B
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EIF4B
NextProtP23588 [Medical]
Target ValidationEIF4B
Huge Navigator EIF4B [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDEIF4B
Pharm GKB GenePA27713
Clinical trialEIF4B
DataMed IndexEIF4B
PubMed154 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Jan 20 14:06:21 CET 2022

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