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. 2021 May 11;4(3):596–606. doi: 10.20517/cdr.2021.20

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© The Author(s) 2021.

© The Author(s) 2021. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing, adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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PI3K/mTOR pathway and regulation of eIF4F complex. (A) PI3K and its downstream effectors AKT and mTOR are activated by many extracellular stimuli. The serine/threonine protein kinase mTOR forms, by association with several binding partners (mLST8, Raptor/Rictor, and mSIN1), 2 distinct complexes mTORC1 and mTORC2. mTORC2 activation leads to actin regulation and cytoskeleton organization, while mTORC1 allows the cap-dependent translation through the 4E-BPs phosphorylation, resulting in the dissociation of these proteins from eIF4E. PI3K pathway dysregulation results in an altered proliferation, carcinogenesis, and angiogenesis. (B) The cap-binding protein eIF4E is released by 4E-BPs as a result of its phosphorylation by mTORC1, allowing eIF4F complex formation and thus permitting translation of eIF4E-sensitive mRNAs.