Erk phosphorylates threonine 42 residue of ribosomal protein S3

Hag Dong Kim, Jae Yung Lee, Joon Kim

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


The ribosomal protein S3 (rpS3) is involved in ribosome biogenesis as a member of ribosomal small subunit and also plays a role in the repair of damaged DNA. Extracellular signal-regulated kinase (Erk), a MAP kinase, is known to play important roles in the regulation of cell growth, differentiation, and apoptosis. In this study, the sequence analysis of rpS3 protein revealed that this protein has a putative FXFP motif which is believed to be an Erk binding site. Indeed, the motif was demonstrated as an Erk binding site by co-immunoprecipitation. In addition to this, it was revealed that Erk specifically phosphorylated Thr 42 residue of rpS3 in vitro and in vivo using the various mutants of rpS3. Taken together, rpS3 appears to be phosphorylated by activated Erk in proliferating cells, resulting in the decreased interaction between two proteins.

Original languageEnglish
Pages (from-to)110-115
Number of pages6
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2005 Jul 22


  • Erk
  • FXFP motif
  • Phosphorylation
  • Threonine residue
  • rpS3

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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