Disruption of microRNA biogenesis confers resistance to ER stress-induced cell death upstream of the mitochondrion

PLoS One. 2013 Aug 19;8(8):e73870. doi: 10.1371/journal.pone.0073870. eCollection 2013.

Abstract

Global downregulation of microRNAs (miRNAs) is a common feature of human tumors and has been shown to enhance cancer progression. Several components of the miRNA biogenesis machinery (XPO5, DICER and TRBP) have been shown to act as haploinsufficient tumor suppressors. How the deregulation of miRNA biogenesis promotes tumor development is not clearly understood. Here we show that loss of miRNA biogenesis increased resistance to endoplasmic reticulum (ER) stress-induced cell death. We observed that HCT116 cells with a DICER hypomorphic mutation (Exn5/Exn5) or where DICER or DROSHA were knocked down were resistant to ER stress-induced cell death. Extensive analysis revealed little difference in the unfolded protein response (UPR) of WT compared to Exn5/Exn5 HCT116 cells upon ER stress treatment. However, analysis of the intrinsic apoptotic pathway showed that resistance occurred upstream of the mitochondria. In particular, BAX activation and dissipation of mitochondrial membrane potential was attenuated, and there was altered expression of BCL-2 family proteins. These observations demonstrate a key role for miRNAs as critical modulators of the ER stress response. In our model, downregulation of miRNA biogenesis delays ER stress-induced apoptosis. This suggests that disrupted miRNA biogenesis may contribute to cancer progression by inhibiting ER stress-induced cell death.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Death
  • Endoplasmic Reticulum Stress / genetics*
  • HCT116 Cells
  • Humans
  • MicroRNAs / biosynthesis*
  • Mitochondria / metabolism*
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • RNA, Small Interfering / metabolism
  • Ribonuclease III / metabolism
  • Unfolded Protein Response

Substances

  • MicroRNAs
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Small Interfering
  • DROSHA protein, human
  • Ribonuclease III

Grants and funding

This work was supported by the following research grants: Breast Cancer campaign, UK (Grant number 2008NovPhD21), URL: www.breastcancercampaign.org; Science foundation Ireland (Grant number 09/RFP/BIC2371or 09/RFP/BMT2153) URL: www.sfi.ie; and the Thomas Crawford Hayes fund, School of Natural Sciences, NUI Galway, Ireland. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.