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c-Src activates endonuclease-mediated mRNA decay

Yong Peng1, Daniel R Schoenberg

  • 1Department of Molecular and Cellular Biochemistry, The RNA Group and the Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, USA.

Molecular Cell
|March 14, 2007
PubMed

Insights

The protein c-Src activates mRNA decay by phosphorylating PMR1, a key enzyme in the process. This discovery links signal transduction pathways to mRNA degradation.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • The mRNA endonuclease PMR1 initiates mRNA decay.
  • PMR1's targeting to polysomes and decay activation depend on tyrosine phosphorylation at position 650.

Purpose of the Study:

  • To identify the kinase responsible for PMR1 phosphorylation.
  • To elucidate the mechanism linking signal transduction to mRNA decay.

Main Methods:

  • Immunoprecipitation to detect PMR1-c-Src complex formation.
  • In vitro and in vivo phosphorylation assays.
  • Analysis of PMR1 activity in cells with varying c-Src levels.
  • Epidermal Growth Factor (EGF) stimulation experiments.

Main Results:

  • c-Src was identified as the kinase phosphorylating PMR1.
  • c-Src interacts with PMR1 via Y650 and N-terminal SH3-binding motifs.
  • Active c-Src is required for PMR1 polysome targeting and mRNA decay.
  • EGF stimulation rapidly induces c-Src-mediated PMR1 phosphorylation.

Conclusions:

  • c-Src is the specific kinase that activates the PMR1-mediated mRNA decay pathway.
  • This study establishes a direct link between tyrosine kinase signaling and mRNA degradation processes.

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