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Angiogenin-Induced tRNA Fragments Inhibit Translation Initiation

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Ivanov, Pavel, Emara, Mohamed M., Villen, Judit, Gygi, Steven P., Anderson, Paul·2011·Molecular Cell

Abstract

SUMMARY Angiogenin is a stress-activated ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs). Transfection of natural or synthetic tiRNAs inhibits protein synthesis and triggers the phospho-eIF2α independent assembly of stress granules (SGs), essential components of the stress response program. We show that selected tiRNAs inhibit protein synthesis by displacing eIF4G/eIF4A from uncapped>capped RNAs. tiRNAs also displace eIF4F, but not eIF4E:4EBP1, from isolated m7G cap. We identify a terminal oligoguanine motif that is required to displace the eIF4F complex, inhibit translation, and induce SG assembly. We show that the tiRNA-associated translational silencer YB-1 contributes to angiogenin-, tiRNA-, and oxidative stress-induced translational repression. Our data reveal some of the mechanisms by which stress-induced tRNA cleavage inhibits protein synthesis and activates a cytoprotective stress response program.

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Metadata

Authors
Ivanov, P., Emara, M. M., Villen, J., Gygi, S. P., & Anderson, P.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2011-08
Volume
43
Issue
4
Pages
613-623
ISSN
1097-2765 (ISSN-L)
OpenAlex
W2056831129
Cited by
985
References
2
FWCI
12.93
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Angiogenin-Induced tRNA Fragments Inhibit Translation Initiation. https://app.cochat.ai/papers/10.1016/j.molcel.2011.06.022
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Ivanov, P., Emara, M. M., Villen, J., Gygi, S. P., & Anderson, P. (2011). Angiogenin-Induced tRNA Fragments Inhibit Translation Initiation. Molecular Cell. https://doi.org/10.1016/j.molcel.2011.06.022

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