EIF4EBP1

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Eukaryotic translation initiation factor 4E binding protein 1
Identifiers
Symbol(s) EIF4EBP1; 4EBP1; BP-1; MGC4316; PHAS-I
External IDs OMIM: 602223 MGI: 103267 HomoloGene: 3021
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1978 13685
Ensembl ENSG00000187840 ENSMUSG00000031490
Uniprot Q13541 Q3TII9
Refseq NM_004095 (mRNA)
NP_004086 (protein)		 NM_007918 (mRNA)
NP_031944 (protein)
Location Chr 8: 38.01 - 38.04 Mb Chr 8: 28.73 - 28.74 Mb
Pubmed search [1] [2]

Eukaryotic translation initiation factor 4E binding protein 1, also known as EIF4EBP1, is a human gene.

This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation.[1]

[edit] References

  1. ^ Entrez Gene: EIF4EBP1 eukaryotic translation initiation factor 4E binding protein 1.

[edit] Further reading

  • Armengol G, Rojo F, Castellví J, et al. (2007). "4E-binding protein 1: a key molecular "funnel factor" in human cancer with clinical implications.". Cancer Res. 67 (16): 7551–5. doi:10.1158/0008-5472.CAN-07-0881. PMID 17699757. 
  • Mader S, Lee H, Pause A, Sonenberg N (1995). "The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins.". Mol. Cell. Biol. 15 (9): 4990–7. PMID 7651417. 
  • Pause A, Belsham GJ, Gingras AC, et al. (1994). "Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function.". Nature 371 (6500): 762–7. doi:10.1038/371762a0. PMID 7935836. 
  • Haystead TA, Haystead CM, Hu C, et al. (1994). "Phosphorylation of PHAS-I by mitogen-activated protein (MAP) kinase. Identification of a site phosphorylated by MAP kinase in vitro and in response to insulin in rat adipocytes.". J. Biol. Chem. 269 (37): 23185–91. PMID 8083223. 
  • Haghighat A, Mader S, Pause A, Sonenberg N (1996). "Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E.". EMBO J. 14 (22): 5701–9. PMID 8521827. 
  • Feigenblum D, Schneider RJ (1996). "Cap-binding protein (eukaryotic initiation factor 4E) and 4E-inactivating protein BP-1 independently regulate cap-dependent translation.". Mol. Cell. Biol. 16 (10): 5450–7. PMID 8816458. 
  • Rousseau D, Gingras AC, Pause A, Sonenberg N (1997). "The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth.". Oncogene 13 (11): 2415–20. PMID 8957083. 
  • Tsukiyama-Kohara K, Vidal SM, Gingras AC, et al. (1997). "Tissue distribution, genomic structure, and chromosome mapping of mouse and human eukaryotic initiation factor 4E-binding proteins 1 and 2.". Genomics 38 (3): 353–63. doi:10.1006/geno.1996.0638. PMID 8975712. 
  • Fadden P, Haystead TA, Lawrence JC (1997). "Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes.". J. Biol. Chem. 272 (15): 10240–7. PMID 9092573. 
  • Brunn GJ, Fadden P, Haystead TA, Lawrence JC (1998). "The mammalian target of rapamycin phosphorylates sites having a (Ser/Thr)-Pro motif and is activated by antibodies to a region near its COOH terminus.". J. Biol. Chem. 272 (51): 32547–50. PMID 9405468. 
  • Burnett PE, Barrow RK, Cohen NA, et al. (1998). "RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1.". Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1432–7. PMID 9465032. 
  • New L, Jiang Y, Zhao M, et al. (1998). "PRAK, a novel protein kinase regulated by the p38 MAP kinase.". EMBO J. 17 (12): 3372–84. doi:10.1093/emboj/17.12.3372. PMID 9628874. 
  • Heesom KJ, Avison MB, Diggle TA, Denton RM (1999). "Insulin-stimulated kinase from rat fat cells that phosphorylates initiation factor 4E-binding protein 1 on the rapamycin-insensitive site (serine-111).". Biochem. J. 336 ( Pt 1): 39–48. PMID 9806882. 
  • Waskiewicz AJ, Johnson JC, Penn B, et al. (1999). "Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo.". Mol. Cell. Biol. 19 (3): 1871–80. PMID 10022874. 
  • Seeley TW, Wang L, Zhen JY (1999). "Phosphorylation of human MAD1 by the BUB1 kinase in vitro.". Biochem. Biophys. Res. Commun. 257 (2): 589–95. doi:10.1006/bbrc.1999.0514. PMID 10198256. 
  • Gingras AC, Gygi SP, Raught B, et al. (1999). "Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism.". Genes Dev. 13 (11): 1422–37. PMID 10364159. 
  • Yang D, Brunn GJ, Lawrence JC (1999). "Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR.". FEBS Lett. 453 (3): 387–90. PMID 10405182. 
  • Kim ST, Lim DS, Canman CE, Kastan MB (2000). "Substrate specificities and identification of putative substrates of ATM kinase family members.". J. Biol. Chem. 274 (53): 37538–43. PMID 10608806. 
  • Mothe-Satney I, Yang D, Fadden P, et al. (2000). "Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression.". Mol. Cell. Biol. 20 (10): 3558–67. PMID 10779345. 
  • Mothe-Satney I, Brunn GJ, McMahon LP, et al. (2000). "Mammalian target of rapamycin-dependent phosphorylation of PHAS-I in four (S/T)P sites detected by phospho-specific antibodies.". J. Biol. Chem. 275 (43): 33836–43. doi:10.1074/jbc.M006005200. PMID 10942774. 
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