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

Hee Sae Park; Jung Soon Mo; Eui Ju Choi

doi:10.1016/j.bbrc.2006.10.034

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

Hee Sae Park, Jung Soon Mo, Eui Ju Choi

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29 Citations (Scopus)

Abstract

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 N^G-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 language	English
Pages (from-to)	281-286
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	351
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2006.10.034
Publication status	Published - 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).

Keywords

JNK
NO
Nitrosylation
c-Jun

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.10.034

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title = "Nitric oxide inhibits an interaction between JNK1 and c-Jun through nitrosylation",

abstract = "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.",

keywords = "JNK, NO, Nitrosylation, c-Jun",

author = "Park, {Hee Sae} and Mo, {Jung Soon} and Choi, {Eui Ju}",

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).",

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AU - Choi, Eui Ju

N1 - 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).

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N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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