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Translation Efficiency and Degradation of ER-Associated mRNAs Modulated by ER-Anchored poly(A)-Specific Ribonuclease

Tian-Li Duan1, Han Jiao1, Guang-Jun He1

  • 1State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.

Cells
|January 16, 2020
PubMed

Insights

Endoplasmic reticulum (ER)-anchored poly(A)-specific ribonuclease (PARN) shortens mRNA poly(A) tails, triggering degradation of specific ER-enriched transcripts and modulating translation efficiency during DNA damage response.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Endoplasmic reticulum (ER)-associated mRNAs typically undergo efficient translation.
  • The precise mechanisms of mRNA deadenylation and degradation at the ER surface remain unclear.

Purpose of the Study:

  • To investigate the presence and function of deadenylases, specifically poly(A)-specific ribonuclease (PARN), on the ER surface.
  • To elucidate the role of ER-anchored PARN in mRNA regulation, translation efficiency, and cellular responses.

Main Methods:

  • Detection of active deadenylases, including PARN, in ER fractions from cell lines and mouse tissues.
  • Biochemical assays using Langmuir monolayers and liposomes to assess PARN's interaction with membranes.
  • Transcriptome sequencing to analyze the impact of ER-anchored PARN on RNA populations.
  • Analysis of ribosome occupancy and polysome profiles to evaluate translation modulation.
  • Investigation of PARN phosphorylation by MK2 during DNA damage response.

Main Results:

  • ER possesses active deadenylases, notably PARN, which can associate with the ER membrane.
  • ER-anchored PARN reshapes poly(A) tail length of ER-associated RNAs, primarily by shortening long tails, without affecting global translation efficiency.
  • ER-anchored PARN promotes the degradation of a subset of ER-enriched transcripts and modulates translation by redistributing ribosomes.
  • Phosphorylation of PARN by MK2 during DNA damage induces its translocation from the ER to the cytosol.
  • ER-anchored PARN influences DNA damage response and cell viability by regulating the decay of ER-associated MDM2 transcripts.

Conclusions:

  • PARN is an ER-anchored deadenylase that regulates mRNA degradation and translation efficiency at the ER surface.
  • ER-anchored PARN plays a role in dynamic ribosome reallocation and cellular responses to DNA damage.
  • A regulated communication exists between mRNA degradation rates and translation efficiency on the ER surface, involving PARN.
Keywords:
DNA damage responseER-anchored ribonucleaseER-associated mRNAsdeadenylationmRNA decaypoly(A) length profilepoly(A)-specific ribonucleasetranslation efficiency

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