Downregulation of miR-17-92 Cluster by PERK Fine-Tunes Unfolded Protein Response Mediated Apoptosis.
Danielle E ReadAnanya GuptaKaren CawleyLaura FontanaPatrizia AgostinisAfshin SamaliSanjeev GuptaPublished in: Life (Basel, Switzerland) (2021)
An important event in the unfolded protein response (UPR) is activation of the endoplasmic reticulum (ER) kinase PERK. The PERK signalling branch initially mediates a prosurvival response, which progresses to a proapoptotic response upon prolonged ER stress. However, the molecular mechanisms of PERK-mediated cell death are not well understood. Here we show that expression of the primary miR-17-92 transcript and mature miRNAs belonging to the miR-17-92 cluster are decreased during UPR. We found that miR-17-92 promoter reporter activity was reduced during UPR in a PERK-dependent manner. Furthermore, we show that activity of the miR-17-92 promoter is repressed by ectopic expression of ATF4 and NRF2. Promoter deletion analysis mapped the region responding to UPR-mediated repression to a site in the proximal region of the miR-17-92 promoter. Hypericin-mediated photo-oxidative ER damage reduced the expression of miRNAs belonging to the miR-17-92 cluster in wild-type but not in PERK-deficient cells. Importantly, ER stress-induced apoptosis was inhibited upon miR-17-92 overexpression in SH-SY5Y and H9c2 cells. Our results reveal a novel function for ATF4 and NRF2, where repression of the miR-17-92 cluster plays an important role in ER stress-mediated apoptosis. Mechanistic details are provided for the potentiation of cell death via sustained PERK signalling mediated repression of the miR-17-92 cluster.
Keyphrases
- endoplasmic reticulum stress
- cell proliferation
- induced apoptosis
- endoplasmic reticulum
- long non coding rna
- long noncoding rna
- poor prognosis
- cell death
- transcription factor
- oxidative stress
- dna methylation
- gene expression
- signaling pathway
- binding protein
- small molecule
- rna seq
- air pollution
- pi k akt
- single cell
- breast cancer cells
- amino acid
- protein protein