Wikipedia

EIF3D

Eukaryotic translation initiation factor 3 subunit D (eIF3d) is a protein that in humans is encoded by the EIF3D gene.[5][6]

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

8664

55944

Ensembl

ENSG00000100353

ENSMUSG00000016554

UniProt

O15371

O70194

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
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Eukaryotic translation initiation factor-3 (eIF3), the largest of the eIFs, is a multiprotein complex composed of at least ten nonidentical subunits. The complex binds to the 40S ribosome and 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 the ternary complex of eIF2/GTP/methionyl-tRNA, and by promoting mRNA binding. 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 to interact with PHLDA1[7] and EIF3A.[8][9][10]

EIF3D has also been shown to interact with c-Jun mRNA 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 as c-Jun which 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 of c-Jun under 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. ^ a b c GRCh38: Ensembl release 89: ENSG00000100353 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016554 – Ensembl, 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. PMID 9341143.
  6. ^ a b "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. PMID 11369516.
  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. PMC 1847948. PMID 17353931.
  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. PMID 14519125.
  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. PMID 9822659.
  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. PMC 5003174. PMID 27462815.
  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. PMID 33417853. S2CID 231303797.
  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. PMID 33184215. S2CID 226308112.

Further reading

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