Related Experiment Video

Updated: Aug 12, 2025

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
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Phosphorylation of rpS3 by Lyn increases translation of Multi-Drug Resistance (MDR1) gene

Woo Sung Ahn1, Hag Dong Kim2, Tae Sung Kim1

  • 1Laboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul 02841, Korea.

BMB Reports
|February 1, 2023
PubMed

Insights

Lyn tyrosine kinase phosphorylates ribosomal protein S3 (RpS3), enhancing p-glycoprotein translation and increasing multidrug resistance. This interaction reveals a novel mechanism in cellular drug resistance.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Lyn is a tyrosine kinase activated by DNA damage, regulating key cellular processes.
  • Ribosomal protein S3 (RpS3) has endonuclease activity for DNA repair and is part of protein biosynthesis.
  • Multidrug resistance (MDR) is a significant challenge in cancer therapy, often mediated by p-glycoprotein.

Discussion:

  • This study reveals a direct interaction between Lyn and RpS3.
  • Lyn phosphorylates RpS3 at the Y167 residue, influencing ribosome function and protein translation.
  • This phosphorylation event upregulates the translation of p-glycoprotein, a key mediator of MDR.

Key Insights:

  • RpS3 acts as a substrate for Lyn, with distinct protein regions interacting with Lyn's SH1 and SH3 domains.
  • The phosphorylation of RpS3 by Lyn is regulated by both the kinase and doxorubicin.
  • This Lyn-mediated phosphorylation of RpS3 enhances cellular drug resistance by increasing p-glycoprotein translation.

Outlook:

  • Further investigation into the structural basis of the Lyn-RpS3 interaction could yield new therapeutic targets.
  • Understanding this pathway may lead to strategies to overcome drug resistance in cancer.
  • Exploring the role of ribosome heterogeneity in drug resistance warrants further study.

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