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
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

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

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

References

  1. GRCh38: Ensembl release 89: ENSG00000100353 - Ensembl, May 2017
  2. 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. "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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