ArticleThe Journal of biological chemistry2016
Translation Regulation of the Glutamyl-prolyl-tRNA Synthetase Gene EPRS through Bypass of Upstream Open Reading Frames with Noncanonical Initiation Codons.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Recent advancements in NRF2-regulated ferroptosis modulation for targeted cancer therapy.Molecular biology reports · 2026Review
- Programmable initiation of mRNA translation by trans-RNA.Nature biotechnology · 2025Article
- Alternative translation initiation produces synaptic organizer proteoforms with distinct localization and functions.Molecular cell · 2024Article
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- Surviving and Adapting to Stress: Translational Control and the Integrated Stress Response.Antioxidants & redox signaling · 2023Review
- Translational control of murine adiponectin expression by an upstream open reading frame element.RNA biology · 2023Article
- Translational buffering by ribosome stalling in upstream open reading frames.PLoS genetics · 2022Article
- Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response.The Journal of biological chemistry · 2021Article
- Translation ofBiomedicines · 2021Article
- Mechanisms of repeat-associated non-AUG translation in neurological microsatellite expansion disorders.Biochemical Society transactions · 2021Review
- Regulation of human sphingomyelin synthase 1 translation through its 5'-untranslated region.FEBS letters · 2020Article
- Roles of the Translation Initiation Factor eIF2α Phosphorylation in Cell Structure and Function.Cell structure and function · 2020Article
- Review
- Pathological mechanisms and therapeutic outlooks for arthrofibrosis.Bone research · 2019Article
- Breast tumor cell hybrids form spontaneouslyAPL bioengineering · 2018Article
- Role of eIF2α Kinases in Translational Control and Adaptation to Cellular Stress.Cold Spring Harbor perspectives in biology · 2018Review
- Translational control of a humanMolecular biology of the cell · 2018Article
- RAN translation at C9orf72-associated repeat expansions is selectively enhanced by the integrated stress response.Nature communications · 2017Article
- An RNA structure-mediated, posttranscriptional model of human α-1-antitrypsin expression.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In the integrated stress response, phosphorylation of eIF2α (eIF2α-P) reduces protein synthesis while concomitantly promoting preferential translation of specific transcripts associated with stress adaptation. Translation of the glutamyl-prolyl-tRNA synthetase gene EPRS is enhanced in response to eIF2α-P. To identify the underlying mechanism of translation control, we employed biochemical approaches to determine the regulatory features by which upstream ORFs (uORFs) direct downstream translation control and expression of the EPRS coding region. Our findings reveal that translation of two inhibitory uORFs encoded by noncanonical CUG and UUG initiation codons in the EPRS mRNA 5'-leader serve to dampen levels of translation initiation at the EPRS coding region. By a mechanism suggested to involve increased translation initiation stringency during stress-induced eIF2α-P, we observed facilitated ribosome bypass of these uORFs, allowing for increased translation of the EPRS coding region. Importantly, EPRS protein expression is enhanced through this preferential translation mechanism in response to multiple known activators of eIF2α-P and likely serves to facilitate stress adaptation in response to a variety of cellular stresses. The rules presented here for the regulated ribosome bypass of noncanonical initiation codons in the EPRS 5'-leader add complexity into the nature of uORF-mediated translation control mechanisms during eIF2α-P and additionally illustrate the roles that previously unexamined uORFs with noncanonical initiation codons can play in modulating gene expression.
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