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- W4380743043 abstract "The heme-regulated kinase HRI is activated under heme/iron deficient conditions; however, the underlying molecular mechanism is incompletely understood. Here, we show that iron-deficiency-induced HRI activation requires the mitochondrial protein DELE1. Notably, mitochondrial import of DELE1 and its subsequent protein stability are regulated by iron availability. Under steady-state conditions, DELE1 is degraded by the mitochondrial matrix-resident protease LONP1 soon after mitochondrial import. Upon iron chelation, DELE1 import is arrested, thereby stabilizing DELE1 on the mitochondrial surface to activate the HRI-mediated integrated stress response (ISR). Ablation of this DELE1-HRI-ISR pathway in an erythroid cell model enhances cell death under iron-limited conditions, suggesting a cell-protective role for this pathway in iron-demanding cell lineages. Our findings highlight mitochondrial import regulation of DELE1 as the core component of a previously unrecognized mitochondrial iron responsive pathway that elicits stress signaling following perturbation of iron homeostasis." @default.
- W4380743043 created "2023-06-16" @default.
- W4380743043 creator A5007297638 @default.
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- W4380743043 creator A5078318814 @default.
- W4380743043 date "2023-06-01" @default.
- W4380743043 modified "2023-10-02" @default.
- W4380743043 title "A mitochondrial iron-responsive pathway regulated by DELE1" @default.
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- W4380743043 doi "https://doi.org/10.1016/j.molcel.2023.05.031" @default.
- W4380743043 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37327776" @default.
- W4380743043 hasPublicationYear "2023" @default.
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