Nitric oxide inhibits an interaction between JNK1 and c-Jun through nitrosylation

Hee Sae Park, Jung Soon Mo, Eui Ju Choi

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)


Nitric oxide (NO) has been shown to negatively regulate c-Jun N-terminal kinase (JNK) through S-nitrosylation. Here, we show that disruption of an interaction between JNK and its substrate c-Jun is an important mechanism underlying the NO-mediated inhibition of JNK signaling. Endogenous NO, which was generated by interferon-γ treatment, suppressed anisomycin-stimulated JNK activity in microglial BV-2 cells. The interferon-γ-induced suppression of JNK1 activation in BV-2 cells was prevented completely by treatment with NG-nitro-l-arginine, an inhibitor of NO synthase. A NO donor S-nitro-N-acetyl-dl-penicillamine (SNAP) inhibited JNK activity in vitro, and this inhibition was reversed by a thiol-reducing agent, dithiothreitol. Nitric oxide disrupts a physical interaction between JNK and its substrate c-Jun both in vitro and in intact cells without affecting an interaction between SEK1 and JNK. Collectively, our results suggest that the inhibition of the interaction between JNK and c-Jun may be an integral part of the mechanism underlying the negative regulation of the JNK signaling pathway by NO.

Original languageEnglish
Pages (from-to)281-286
Number of pages6
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2006 Dec 8

Bibliographical note

Funding Information:
We thank Dr. R.J. Davis for JNK cDNAs, and Dr. L.I. Zon for SEK1 cDNA. This work was supported by the Molecular and Cellular BioDiscovery Research Program Grant (M10601000136-06N0100-13610) from the Ministry of Science and Technology, South Korea (E.-J.C.) and Korea Research Foundation Grant (KRF-1999-005-C00026) funded by the Korean Government (H.-S..P).


  • JNK
  • NO
  • Nitrosylation
  • c-Jun

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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