ArticleAmerican journal of physiology. Renal physiology2011
Phosphorylation of eIF2α via the general control kinase, GCN2, modulates the ability of renal medullary cells to survive high urea stress.
Article in American journal of physiology. Renal physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Multiple Roles of the Stress Sensor GCN2 in Immune Cells.International journal of molecular sciences · 2023Review
- Collective Learnings of Studies of Stress Granule Assembly and Composition.Methods in molecular biology (Clifton, N.J.) · 2022Article
- tRNA fragmentation and protein translation dynamics in the course of kidney injury.RNA biology · 2018Review
- Indoleamine 2, 3-dioxygenase (IDO) increases during renal fibrogenesis and its inhibition potentiates TGF-β 1-induced epithelial to mesenchymal transition.BMC nephrology · 2017Article
- Protein Kinase R Mediates the Inflammatory Response Induced by Hyperosmotic Stress.Molecular and cellular biology · 2017Article
- WNK Kinases in Development and Disease.Current topics in developmental biology · 2017Review
- Epithelial sodium channel abundance is decreased by an unfolded protein response induced by hyperosmolality.Physiological reports · 2014Article
- Phosphorylation of eIF2α attenuates statin-induced apoptosis by inhibiting the stabilization and translocation of p53 to the mitochondria.International journal of oncology · 2013Article
- GCN-2 dependent inhibition of protein synthesis activates osmosensitive gene transcription via WNK and Ste20 kinase signaling.American journal of physiology. Cell physiology · 2012Article
- Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism.Advances in nutrition (Bethesda, Md.) · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The phosphorylation of the α-subunit of the eukaryotic translation initiation factor 2 (eIF2α) occurs under many stress conditions in mammalian cells and is mediated by one of four eIF2α kinases: PERK, PKR, GCN2, and HRI. Cells of the renal medulla are regularly exposed to fluctuating concentrations of urea and sodium, the extracellular solutes responsible for the high osmolality in the renal medulla, and thus the kidneys ability to concentrate the urine in times of dehydration. Urea stress is known to initiate molecular responses that diverge from those seen in response to hypertonic stress (NaCl). We show that urea-inducible GCN2 activation initiates the phosphorylation of eIF2α and the downstream increase of activating transcription factor 3 (ATF3). Loss of GCN2 sensitized cells to urea stress, increasing the expression of activated caspase-3 and decreasing cell survival. Loss of GCN2 ablated urea-induced phosphorylation of eIF2α and reduced the expression of ATF3.
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Registered trials
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