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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The mammalian target of rapamycin (mTOR) pathway is crucial for regulating cell growth and protein synthesis.
  • mTOR controls protein synthesis partly through messenger RNAs (mRNAs) with a 5' terminal oligopyrimidine tract (TOP).
  • The precise mechanisms linking mTOR signaling to TOP mRNA regulation remain incompletely understood.

Purpose of the Study:

  • To investigate the impact of mTOR inhibition on the RNA-binding protein (RBP) landscape.
  • To identify proteins interacting with mRNAs regulated by mTOR.
  • To elucidate the role of LARP1 and PABPC1 in mTOR-mediated translational control.

Main Methods:

  • RNA-binding protein (RBP) capture assays were employed to analyze protein-RNA interactions.
  • Changes in protein binding to mRNAs were assessed following mTOR inhibition.
  • The interaction of LARP1 with TOP and non-TOP mRNAs was examined.
  • The role of PABPC1 in LARP1-mRNA association was investigated.

Main Results:

  • mTOR inhibition led to increased binding of LARP1 to various mRNAs, including TOP-containing ones.
  • LARP1 binding to non-TOP mRNAs resulted in translational repression, even without mTOR inhibition.
  • A significant overlap was observed between the mRNA interactomes of LARP1 and PABPC1.
  • PABPC1 was found to be essential for LARP1's association with its target mRNAs.
  • mRNAs bound by both LARP1 and PABPC1, including those for cell growth proteins, were translationally repressed.

Conclusions:

  • LARP1 acts as a key regulator of mRNA translation downstream of mTOR signaling.
  • The complex of LARP1 and PABPC1 plays a critical role in repressing the translation of specific mRNAs.
  • This mechanism highlights a novel pathway for controlling protein synthesis related to cell growth and survival.