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Phosphorylation of Y14 modulates its interaction with proteins involved in mRNA metabolism and influences its

Ia-Wen Hsu1, Min Hsu, Chin Li

  • 1Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan.

The Journal of Biological Chemistry
|August 16, 2005
PubMed

Insights

Phosphorylation of Y14, an exon junction complex (EJC) component, disrupts its interactions, impacting mRNA surveillance. Methylation and phosphorylation of Y14 show antagonistic regulation, suggesting roles in remodeling messenger ribonucleoproteins (mRNPs).

Area of Science:

  • Molecular Biology
  • RNA Biology
  • Post-translational Modifications

Background:

  • The exon junction complex (EJC) is crucial for post-splicing mRNA processing, including export, nonsense-mediated mRNA decay (NMD), and translation control.
  • Y14 is a core component of the EJC, playing a significant role in these post-splicing events.

Purpose of the Study:

  • To identify and characterize post-translational modifications of the EJC core component Y14.
  • To investigate the functional consequences of Y14 phosphorylation and methylation on EJC assembly and function.

Main Methods:

  • Analysis of Y14 phosphorylation at arginine/serine (RS) dipeptides using biochemical assays.
  • Characterization of a non-phosphorylatable Y14 mutant in association with spliced mRNA and NMD activation.
  • Investigation of Y14 methylation in the carboxyl-terminal domain and its interplay with phosphorylation.

Main Results:

  • Y14 is phosphorylated at RS dipeptides, likely by SR protein-specific kinases, which abolishes its interaction with EJC components and downstream factors.
  • A non-phosphorylatable Y14 mutant associates with spliced mRNA and activates NMD but sequesters EJC and NMD factors on ribosome-containing mRNPs.
  • Y14 methylation occurs at multiple arginine residues and is antagonized by RS dipeptide phosphorylation, suggesting coordinated regulation.

Conclusions:

  • Y14 phosphorylation likely facilitates the dissociation of Y14 from ribosome-containing mRNPs after mRNA surveillance completion.
  • Antagonistic post-translational modifications (phosphorylation and methylation) of Y14 may regulate the remodeling of Y14-containing mRNPs.

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