Plasticity of nuclear and cytoplasmic stress responses of RNA-binding proteins

Nucleic Acids Res. 2020 May 21;48(9):4725-4740. doi: 10.1093/nar/gkaa256.

Abstract

Cellular stress causes multifaceted reactions to trigger adaptive responses to environmental cues at all levels of the gene expression pathway. RNA-binding proteins (RBP) are key contributors to stress-induced regulation of RNA fate and function. Here, we uncover the plasticity of the RNA interactome in stressed cells, differentiating between responses in the nucleus and in the cytoplasm. We applied enhanced RNA interactome capture (eRIC) analysis preceded by nucleo-cytoplasmic fractionation following arsenite-induced oxidative stress. The data reveal unexpectedly compartmentalized RNA interactomes and their responses to stress, including differential responses of RBPs in the nucleus versus the cytoplasm, which would have been missed by whole cell analyses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Fractionation
  • Cell Line, Tumor
  • Cell Nucleus / metabolism*
  • Cytoplasm / metabolism*
  • Humans
  • Oxidative Stress
  • Protein Biosynthesis
  • RNA Stability
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / metabolism*

Substances

  • RNA, Messenger
  • RNA-Binding Proteins