Перейти в головне навігаційне меню Перейти до головного Перейти на нижній колонтитул сайту

Біологія та біотехнології

September 5, 2025; Boston, USA: VIII Міжнародна науково-практична конференція «SCIENTIFIC PRACTICE: MODERN AND CLASSICAL RESEARCH METHODS»


A COMPARATIVE STUDY OF EIF2А KINASES IN PLANT AND MAMMALIAN ANTIVIRAL RESPONSES


DOI
https://doi.org/10.36074/logos-05.09.2025.017
Опубліковано
05.09.2025

Анотація

Absolutely all living organisms suffer from viruses. This applies to plants as well as to animals. Despite the evolutionary distance between them, each kingdom deploys rapid innate defense mechanisms, relying on translational control and regulating protein synthesis as a key defensive mechanism.

Посилання

  1. Bogorad, A. M., Lin, K. Y., & Marintchev, A. (2017). Novel mechanisms of eIF2B action and regulation by eIF2α phosphorylation. Nucleic Acids Research, 45(20), 11962–11979. https://doi.org/10.1093/nar/gkx845
  2. Cesaro, T., Hayashi, Y., Borghese, F., Vertommen, D., Wavreil, F., & Michiels, T. (2021). PKR activity modulation by phosphomimetic mutations of serine residues located three aminoacids upstream of double-stranded RNA binding motifs. Scientific Reports, 11(1). https://doi.org/10.1038/s41598-021-88610-z
  3. Cnop, M., Toivonen, S., Igoillo-Esteve, M., & Salpea, P. (2017). Endoplasmic reticulum stress and eIF2α phosphorylation: The Achilles heel of pancreatic β cells. Molecular Metabolism, 6(9), 1024–1039. https://doi.org/10.1016/j.molmet.2017.06.001
  4. Ferreira, M. A., Teixeira, R. M., Brustolini, O. J. B., Saia, T. F. F., Jean-Baptiste, J., Ribeiro, N. G. A., Breves, S. S., Sampaio, F. R., Santos, E. G. D., Leon, B. A., Oliveira, C. C., Duarte, C. E. M., Lima, L. L., Oliveira, L. L., Ramos, H. J. O., Reis, P. a. B., & Fontes, E. P. B. (2025). The immune NIK1/RPL10/LIMYB signaling module regulates photosynthesis and translation under biotic and abiotic stresses. Nature Communications, 16(1). https://doi.org/10.1038/s41467-025-59571-y
  5. GarcíA, M. A., Gil, J., Ventoso, I., Guerra, S., Domingo, E., Rivas, C., & Esteban, M. (2006). Impact of Protein Kinase PKR in Cell Biology: from Antiviral to Antiproliferative Action. Microbiology and Molecular Biology Reviews, 70(4), 1032–1060. https://doi.org/10.1128/mmbr.00027-06
  6. Huang, H., Chen, L., Chi, J., Lai, S., Pi, J., Shao, Y., & Xu, J. (2025). Stress granules and cell death: crosstalk and potential therapeutic strategies in infectious diseases. Cell Death and Disease, 16(1). https://doi.org/10.1038/s41419-025-07800-z
  7. Lageix, S., Lanet, E., Pouch-Pélissier, M., Espagnol, M., Robaglia, C., Deragon, J., &
  8. Pélissier, T. (2008a). ArabidopsiseIF2α kinase GCN2 is essential for growth in stress conditions and is activated by wounding. BMC Plant Biology, 8(1). https://doi.org/10.1186/1471-2229-8-134
  9. Lageix, S., Lanet, E., Pouch-Pélissier, M., Espagnol, M., Robaglia, C., Deragon, J., & Pélissier, T. (2008b). ArabidopsiseIF2α kinase GCN2 is essential for growth in stress conditions and is activated by wounding. BMC Plant Biology, 8(1). https://doi.org/10.1186/1471-2229-8-134
  10. Liu, Y., Wang, M., Cheng, A., Yang, Q., Wu, Y., Jia, R., Liu, M., Zhu, D., Chen, S., Zhang, S., Zhao, X., Huang, J., Mao, S., Ou, X., Gao, Q., Wang, Y., Xu, Z., Chen, Z., Zhu, L., . . . Chen, X. (2020). The role of host eIF2α in viral infection. Virology Journal, 17(1). https://doi.org/10.1186/s12985-020-01362-6
  11. Lokdarshi, A., & Von Arnim, A. G. (2022). Review: Emerging roles of the signaling network of the protein kinase GCN2 in the plant stress response. Plant Science, 320, 111280. https://doi.org/10.1016/j.plantsci.2022.111280
  12. Rutkowski, D. T., Kang, S., Goodman, A. G., Garrison, J. L., Taunton, J., Katze, M. G., Kaufman, R. J., & Hegde, R. S. (2007). The role of P58IPK in protecting the stressed endoplasmic reticulum. Molecular Biology of the Cell, 18(9), 3681–3691. https://doi.org/10.1091/mbc.e07-03-0272
  13. Sesma, A., Castresana, C., & Castellano, M. M. (2017). Regulation of translation by TOR, EIF4E and EIF2Α in plants: Current knowledge, challenges and future Perspectives. Frontiers in Plant Science, 8. https://doi.org/10.3389/fpls.2017.00644
  14. Uppala, J. K., Ghosh, C., Sathe, L., & Dey, M. (2018). Phosphorylation of translation initiation factor eIF2α at Ser51 depends on site‐ and context‐specific information. FEBS Letters, 592(18), 3116–3125. https://doi.org/10.1002/1873-3468.13214
  15. Veerapen, V. P. (2024). Investigation of plant responses to foreign double-stranded RNA. https://usherbrooke.scholaris.ca/items/ac55bdb4-92c8-4127-b116-2e3db3d178ec
  16. Vermeulen, A., Takken, F. L. W., & Sánchez-Camargo, V. A. (2023). Translation arrest: a key player in plant antiviral response. Genes, 14(6), 1293. https://doi.org/10.3390/genes14061293
  17. Wang, L., Li, H., Zhao, C., Li, S., Kong, L., Wu, W., Kong, W., Liu, Y., Wei, Y., Zhu, J., & Zhang, H. (2016). The inhibition of protein translation mediated by AtGCN1 is essential for cold tolerance in Arabidopsis thaliana. Plant Cell & Environment, 40(1), 56–68. https://doi.org/10.1111/pce.12826