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EIF4EBP2

Introduction

Eukaryotic translation initiation factor 4E-binding protein 2 is a protein that in humans is encoded by the EIF4EBP2 gene.[1][2][3]

Animal studies

Animal studies

EIF4EBP2 knockout mice have been used as an animal model of autism. Mice without the Eif4ebp2 gene exhibited autism-like symptoms, including poor social interaction, altered communication and repetitive behaviors. Knockout mice have high levels of Neuroligins.[4]

Interactions

Interactions

EIF4EBP2 has been shown to interact with EIF4E.[1][5]

References

References

  1. ↑ 1.0 1.1 Pause A, Belsham GJ, Gingras AC, Donzé O, Lin TA, Lawrence JC, Sonenberg N (November 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.
  2. ↑ Tsukiyama-Kohara K, Vidal SM, Gingras AC, Glover TW, Hanash SM, Heng H, Sonenberg N (1996). “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.
  3. ↑ “Entrez Gene: EIF4EBP2 eukaryotic translation initiation factor 4E binding protein 2”.
  4. ↑ Gkogkas CG, Khoutorsky A, Ran I, Rampakakis E, Nevarko T, Weatherill DB, Vasuta C, Yee S, Truitt M, Dallaire P, Major F, Lasko P, Ruggero D, Nader K, Lacaille JC, Sonenberg N (2013). “Autism-related deficits via dysregulated eIF4E-dependent translational control”. Nature. 493 (7432): 371–7. doi:10.1038/nature11628. PMC 4133997. PMID 23172145. Lay summary – Nature Magazine.
  5. ↑ Mader S, Lee H, Pause A, Sonenberg N (September 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. PMC 230746. PMID 7651417.
Further reading

Further reading

  • Lin TA, Lawrence JC (1996). “Control of the translational regulators PHAS-I and PHAS-II by insulin and cAMP in 3T3-L1 adipocytes”. J. Biol. Chem. 271 (47): 30199–204. doi:10.1074/jbc.271.47.30199. PMID 8939971.
  • Dilling MB, Germain GS, Dudkin L, Jayaraman AL, Zhang X, Harwood FC, Houghton PJ (2002). “4E-binding proteins, the suppressors of eukaryotic initiation factor 4E, are down-regulated in cells with acquired or intrinsic resistance to rapamycin”. J. Biol. Chem. 277 (16): 13907–17. doi:10.1074/jbc.M110782200. PMID 11847216.
  • Shenberger JS, Adams MH, Zimmer SG (2002). “Oxidant-induced hypertrophy of A549 cells is accompanied by alterations in eukaryotic translation initiation factor 4E and 4E-binding protein-1”. Am. J. Respir. Cell Mol. Biol. 27 (2): 250–6. doi:10.1165/ajrcmb.27.2.4785. PMID 12151318.
  • Ferguson G, Mothe-Satney I, Lawrence JC (2003). “Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E”. J. Biol. Chem. 278 (48): 47459–65. doi:10.1074/jbc.M307949200. PMID 14507920.
  • Joshi B, Cameron A, Jagus R (2004). “Characterization of mammalian eIF4E-family members”. Eur. J. Biochem. 271 (11): 2189–203. doi:10.1111/j.1432-1033.2004.04149.x. PMID 15153109.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.