Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation

Chang Young Jang, Hag Dong Kim, Joon Kim

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

It has been reported that ribosomal protein S3 (rpS3) functions as a ribosomal protein, a DNA repair endonuclease, a proapoptotic protein, and an essential subunit of the native NF-κB complex. However, it is unknown how rpS3 induces apoptosis in response to extracellular stresses. We report here that rpS3 sensitizes genotoxic stress-induced apoptosis by activating JNK through a caspase dependent manner. This apoptotic effect was shown to result from the physical interaction between rpS3 and TRADD, as assessed by coimmunoprecipitation. Moreover, GFP-rpS3 colocalized with TRADD around the plasma membrane and in the cytoplasm during apoptosis. Thus, rpS3 appears to be recruited to the death-inducing signaling complex (DISC) to induce apoptosis by interacting TRADD in response to extracellular stresses. Based on the findings of this study, we concluded that rpS3 is recruited to the DISC and plays a critical role in both genotoxic stress and cytokine induced apoptosis.

Original languageEnglish
Pages (from-to)474-478
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume421
Issue number3
DOIs
Publication statusPublished - 2012 May 11

Fingerprint

Caspases
Chemical activation
Apoptosis
Death Domain Receptor Signaling Adaptor Proteins
DNA Damage
Ribosomal Proteins
Endonucleases
Deoxyribonuclease I
Protein Subunits
Cell membranes
ribosomal protein S3
DNA Repair
Cytoplasm
Repair
Cell Membrane
Cytokines
DNA
Proteins

Keywords

  • Apoptosis
  • Caspase
  • JNK
  • RpS3
  • TRADD

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation. / Jang, Chang Young; Kim, Hag Dong; Kim, Joon.

In: Biochemical and Biophysical Research Communications, Vol. 421, No. 3, 11.05.2012, p. 474-478.

Research output: Contribution to journalArticle

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