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EIF3D

From Wikipedia, the free encyclopedia
EIF3D
Identifiers
AliasesEIF3D,EIF3S7, eIF3-p66, eIF3-zeta, eukaryotic translation initiation factor 3 subunit D
External IDsOMIM:603915;MGI:1933181;HomoloGene:2782;GeneCards:EIF3D;OMA:EIF3D - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003753

NM_018749

RefSeq (protein)

NP_003744

NP_061219

Location (UCSC)Chr 22: 36.51 – 36.53 MbChr 15: 77.84 – 77.86 Mb
PubMedsearch[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eukaryotic translation initiation factor 3 subunit D(eIF3d) is aproteinthat in humans is encoded by theEIF3Dgene.[5][6]

Function

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Eukaryotic translation initiation factor-3 (eIF3), the largest of theeIFs,is amultiprotein complexcomposed of at least ten nonidentical subunits. The complex binds to the40S ribosomeand helps maintain the 40S and 60S ribosomal subunits in a dissociated state. It is also thought to play a role in the formation of the 40S initiation complex by interacting with theternary complexof eIF2/GTP/methionyl-tRNA, and by promotingmRNAbinding. The protein encoded by this gene is the major RNA binding subunit of the eIF3 complex.[6]

Interactions

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EIF3D has been shown tointeractwithPHLDA1[7]andEIF3A.[8][9][10]

EIF3D has also been shown to interact withc-JunmRNA via a non-canonical mechanism. Instead of the EIF4G protein acting as a cap-binding protein to mediate translation, EIF3D has been shown to be a cap binding protein for certain mRNAs such asc-Junwhich has structures at the 5' UTR inhibiting binding of EIF4G and promoting binding of EIF3D.[11]EIF3D as a cap binding protein has been thought of as critical to regulating gene expression under cell stress such as during glucose deprivation. For translation ofc-Jununder glucose starved conditions, the cap binding activity of EIF3D increased by 10-fold.[12][13]

See also

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References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000100353Ensembl,May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000016554Ensembl,May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (October 1997)."Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly".The Journal of Biological Chemistry.272(43): 27042–27052.doi:10.1074/jbc.272.43.27042.PMID9341143.
  6. ^ab"Entrez Gene: EIF3S7 eukaryotic translation initiation factor 3, subunit 7 zeta, 66/67kDa".
  7. ^Hinz T, Flindt S, Marx A, Janssen O, Kabelitz D (May 2001). "Inhibition of protein synthesis by the T cell receptor-inducible human TDAG51 gene product".Cellular Signalling.13(5): 345–352.doi:10.1016/S0898-6568(01)00141-3.PMID11369516.
  8. ^Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007)."Large-scale mapping of human protein-protein interactions by mass spectrometry".Molecular Systems Biology.3(1): 89.doi:10.1038/msb4100134.PMC1847948.PMID17353931.
  9. ^Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (October 2003)."Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3".European Journal of Biochemistry.270(20): 4133–4139.doi:10.1046/j.1432-1033.2003.03807.x.PMID14519125.
  10. ^Block KL, Vornlocher HP, Hershey JW (November 1998)."Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3".The Journal of Biological Chemistry.273(48): 31901–31908.doi:10.1074/jbc.273.48.31901.PMID9822659.
  11. ^Lee AS, Kranzusch PJ, Doudna JA, Cate JH (August 2016)."eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation".Nature.536(7614): 96–99.Bibcode:2016Natur.536...96L.doi:10.1038/nature18954.PMC5003174.PMID27462815.
  12. ^Jia L, Qian SB (January 2021)."A Versatile eIF3d in Translational Control of Stress Adaptation".Molecular Cell.81(1): 10–12.doi:10.1016/j.molcel.2020.12.016.PMID33417853.S2CID231303797.
  13. ^Lamper AM, Fleming RH, Ladd KM, Lee AS (November 2020). "A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress".Science.370(6518): 853–856.Bibcode:2020Sci...370..853L.doi:10.1126/science.abb0993.PMID33184215.S2CID226308112.

Further reading

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