Modulation of nonsense mediated decay by rapamycin

Nucleic Acids Res. 2017 Apr 7;45(6):3448-3459. doi: 10.1093/nar/gkw1109.

Abstract

Rapamycin is a naturally occurring macrolide whose target is at the core of nutrient and stress regulation in a wide range of species. Despite well-established roles as an inhibitor of cap-dependent mRNA translation, relatively little is known about its effects on other modes of RNA processing. Here, we characterize the landscape of rapamycin-induced post-transcriptional gene regulation. Transcriptome analysis of rapamycin-treated cells reveals genome-wide changes in alternative mRNA splicing and pronounced changes in NMD-sensitive isoforms. We demonstrate that despite well-documented attenuation of cap-dependent mRNA translation, rapamycin can augment NMD of certain transcripts. Rapamycin-treatment significantly reduces the levels of both endogenous and exogenous Premature Termination Codon (PTC)-containing mRNA isoforms and its effects are dose-, UPF1- and 4EBP-dependent. The PTC-containing SRSF6 transcript exhibits a shorter half-life upon rapamycin-treatment as compared to the non-PTC isoform. Rapamycin-treatment also causes depletion of PTC-containing mRNA isoforms from polyribosomes, underscoring the functional relationship between translation and NMD. Enhanced NMD activity also correlates with an enrichment of the nuclear Cap Binding Complex (CBC) in rapamycin-treated cells. Our data demonstrate that rapamycin modulates global RNA homeostasis by NMD.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing / drug effects
  • Codon, Nonsense
  • Eukaryotic Initiation Factors / physiology
  • HEK293 Cells
  • Humans
  • Nonsense Mediated mRNA Decay / drug effects*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism
  • Polyribosomes / metabolism
  • RNA Helicases
  • RNA Isoforms / metabolism
  • RNA, Messenger / metabolism
  • Serine-Arginine Splicing Factors / genetics
  • Serine-Arginine Splicing Factors / metabolism
  • Sirolimus / pharmacology*
  • Trans-Activators / physiology

Substances

  • Codon, Nonsense
  • Eukaryotic Initiation Factors
  • Phosphoproteins
  • RNA Isoforms
  • RNA, Messenger
  • SRSF6 protein, human
  • Trans-Activators
  • Serine-Arginine Splicing Factors
  • RNA Helicases
  • UPF1 protein, human
  • Sirolimus