Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species

Sumbayev, Vadim V.; Yasinska, Inna M.

doi:10.1016/j.abb.2005.02.021

Cited by 117 publications

(93 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As most of ribosomal proteins are highly basic, they may have a function of controlling the intracellular redox state. Therefore, we supposed that ASK1 activation in aberrant ribosomal biogenesis is triggered by reactive oxygen species generation (Sumbayev and Yasinska, 2005). We also demonstrated that aberrant ribosome biogenesis elicits both p38 activation and p53 phosphorylation at serines 15 and 33 (Figure 2c).…”

Section: Discussionmentioning

confidence: 70%

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

2011

Oncogene

View full text Add to dashboard Cite

The largest energy consumer in the cell is the ribosome biogenesis whose aberrancy elicits various diseases in humans. It has been recently revealed that p53 induction, along with cell cycle arrest, is related with abnormal ribosome biogenesis, but the exact mechanism still remains unknown. In this study, we have found that aberrant ribosome biogenesis activates two parallel cellular pathways, c-Myc and ASK1/p38, which result in p53 induction and G1 arrest. The c-Myc stabilizes p53 by rpL11-mediated HDM2 inhibition, and ASK1/p38 activates p53 by phosphorylation on serine 15 and 33. Our studies demonstrate the relationship between these two pathways and p53 induction. The changes caused by impaired ribosomal stress, such as p53 induction and G1 arrest, were completely disappeared by inhibition of either pathway. These findings suggest a monitoring mechanism of c-Myc and ASK1/p38 against abnormal ribosome biogenesis through controlling the stability and activity of p53 protein.

show abstract

Section: Discussionmentioning

confidence: 70%

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

2011

Oncogene

View full text Add to dashboard Cite

show abstract

“…The mitogen-activated protein kinase kinase kinase apoptosis signal-regulated kinase-1 (Ask1) and its downstream stress-activated kinases p38 and Jun NH 2 -terminal kinase (JNK) constitute an important mammalian signaling pathway that can promote cell survival, apoptosis, proliferation, or differentiation, depending on the cell type and/or cellular context (Takeda et al, 2000;Sayama et al, 2001;Sumbayev and Yasinska, 2005). Ask1 can be activated by H 2 O 2 ; thus, it is part of a redox-signaling pathway (Gotoh and Cooper, 1998;Tobiume et al, 2001;Kadowaki et al, 2005;Noguchi et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…In bacteria, OxyR is an archetypical H 2 O 2 sensor at the top of a redox-sensitive pathway, being activated by H 2 O 2 through formation of an intramolecular disulfide bond and controlling the transcription of antioxidant defense genes (Storz and Tartaglia, 1992;Zheng et al, 1998). In yeast, H 2 O 2 sensing involves the thiol-based peroxidase Orp1/Gpx3, which, upon oxidation by H 2 O 2 , mediates the formation of an intramolecular disulfide bond in the Yap1 transcription factor, causing its activation (Lee et al, 1999;Delaunay et al, 2002).The mitogen-activated protein kinase kinase kinase apoptosis signal-regulated kinase-1 (Ask1) and its downstream stress-activated kinases p38 and Jun NH 2 -terminal kinase (JNK) constitute an important mammalian signaling pathway that can promote cell survival, apoptosis, proliferation, or differentiation, depending on the cell type and/or cellular context (Takeda et al, 2000;Sayama et al, 2001;Sumbayev and Yasinska, 2005). Ask1 can be activated by H 2 O 2 ; thus, it is part of a redox-signaling pathway (Gotoh and Cooper, 1998;Tobiume et al, 2001;Kadowaki et al, 2005;Noguchi et al, 2005).…”

mentioning

confidence: 99%

Disulfide Bond-mediated Multimerization of Ask1 and Its Reduction by Thioredoxin-1 Regulate H₂O₂-induced c-Jun NH₂-terminal Kinase Activation and Apoptosis

Nadeau

Charette

Toledano

et al. 2007

MBoC

173

137

View full text Add to dashboard Cite

Apoptosis signal-regulated kinase-1 (Ask1) lies upstream of a major redox-sensitive pathway leading to the activation of Jun NH 2 -terminal kinase (JNK) and the induction of apoptosis. We found that cell exposure to H 2 O 2 caused the rapid oxidation of Ask1, leading to its multimerization through the formation of interchain disulfide bonds. Oxidized Ask1 was fully reduced within minutes after induction by H 2 O 2 . During this reduction, the thiol-disulfide oxidoreductase thioredoxin-1 (Trx1) became covalently associated with Ask1. Overexpression of Trx1 accelerated the reduction of Ask1, and a redox-inactive mutant of Trx1 (C35S) remained trapped with Ask1, blocking its reduction. Preventing the oxidation of Ask1 by either overexpressing Trx1 or using an Ask1 mutant in which the sensitive cysteines were mutated (Ask1-⌬Cys) impaired the activation of JNK and the induction of apoptosis while having little effect on Ask1 activation. These results indicate that Ask1 oxidation is required at a step subsequent to activation for signaling downstream of Ask1 after H 2 O 2 treatment. INTRODUCTIONH 2 O 2 is emerging as an important intracellular signaling molecule affecting a variety of cellular responses. In mammals, H 2 O 2 concentration transiently increases in response to different membrane-receptor agonists such as peptide growth factors, hormones, cytokines, and neurotransmitters. This increase of H 2 O 2 concentration is important for downstream signaling from the corresponding membrane receptors (Deyulia et al., 2005;Rhee et al., 2005;Stone and Yang, 2006). Some of these H 2 O 2 regulatory effects are mediated by protein-thiol oxidation, as shown for the oxidative inhibition of protein tyrosine phosphatase upon receptor-tyrosine kinases engagement. H 2 O 2 can oxidize cysteine residues to the sulfenic (protein-SOH), sulfinic (protein-SO 2 H), and sulfonic acid (protein-SO 3 H) forms, also leading to intra-or intermolecular disulfide bonds (protein-SS-protein) and to protein glutathionylation (protein-SSG). Similarly to protein posttranslational modification by serine, threonine, and tyrosine phosphorylation, oxidation of cysteine residues can trigger changes in protein conformation and activity (Filomeni et al., 2005). In bacteria, OxyR is an archetypical H 2 O 2 sensor at the top of a redox-sensitive pathway, being activated by H 2 O 2 through formation of an intramolecular disulfide bond and controlling the transcription of antioxidant defense genes (Storz and Tartaglia, 1992;Zheng et al., 1998). In yeast, H 2 O 2 sensing involves the thiol-based peroxidase Orp1/Gpx3, which, upon oxidation by H 2 O 2 , mediates the formation of an intramolecular disulfide bond in the Yap1 transcription factor, causing its activation (Lee et al., 1999;Delaunay et al., 2002).The mitogen-activated protein kinase kinase kinase apoptosis signal-regulated kinase-1 (Ask1) and its downstream stress-activated kinases p38 and Jun NH 2 -terminal kinase (JNK) constitute an important mammalian signaling pathway that can promote cell surviv...

show abstract

“…JNK has been well established as the key modulator for various stress responses, including nitrosative stress. 9 Although JNK is known to play an important role in RNS-induced apoptosis, 8,10 it remains to be determined whether JNK is also involved in RNS-induced non-apoptotic cell death. In this study, we first observed a relatively slow but sustained JNK activation after SNP treatment: evident JNK activation started from 2 h and reached the peak at 4 h ( Figure 2a).…”

Section: Resultsmentioning

confidence: 99%

“…Second, JNK is known to play an important role in RNS-induced apoptosis. 8 It remains to be determined whether JNK is also involved in RNS-induced non-apoptotic cell death. In this study, we first identified JNK1 as the key effector molecule in RNS-induced caspase-independent non-apoptotic cell death in mouse embryonic fibroblasts (MEF).…”

mentioning

confidence: 99%

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Zhang

et al. 2007

Cell Death Differ

View full text Add to dashboard Cite

At present, the signaling pathways controlling reactive nitrogen species (RNS)-induced non-apoptotic cell death are relatively less understood. In this work, various RNS donors are found to induce caspase-independent non-apoptotic cell death in mouse embryonic fibroblasts (MEF). In search of the molecular mechanisms, we first established the role of c-Jun N-terminal kinase (JNK) in RNS-induced non-apoptotic cell death. RNS readily activate JNK, and the jnk1À/À MEF are resistant to RNS-induced cell death. Moreover, the reconstitution of JNK1 effectively restores the sensitivity to RNS. Next, we identified tumor necrosis factor receptor-associated factor 2 (TRAF2) and apoptosis signal-regulating kinase 1 (ASK1) as the essential upstream molecules for RNS-induced JNK activation and cell death. RNS fail to activate JNK and induce cell death in traf2À/À MEF; and reconstitution of TRAF2 effectively restores the responsiveness of traf2À/À MEF to RNS. Moreover, RNS-induced ASK1 activation is impaired in traf2À/À cells and overexpression of a mutant ASK1 protein suppresses RNS-induced cell death in wild-type MEF cells. Last, we explored the signaling events upstream of TRAF2 and found that translocation of TRAF2 and JNK1 onto membrane lipid rafts is required for RNS-mediated JNK1 activation and cell death. Taken together, data from our study reveal a novel signaling pathway regulating RNS-induced JNK1 activation and non-apoptotic cell death.

show abstract

Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species

Cited by 117 publications

References 53 publications

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

Disulfide Bond-mediated Multimerization of Ask1 and Its Reduction by Thioredoxin-1 Regulate H₂O₂-induced c-Jun NH₂-terminal Kinase Activation and Apoptosis

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Contact Info

Product

Resources

About

Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species

Cited by 117 publications

References 53 publications

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

Aberrant ribosome biogenesis activates c-Myc and ASK1 pathways resulting in p53-dependent G1 arrest

Disulfide Bond-mediated Multimerization of Ask1 and Its Reduction by Thioredoxin-1 Regulate H2O2-induced c-Jun NH2-terminal Kinase Activation and Apoptosis

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Contact Info

Product

Resources

About

Disulfide Bond-mediated Multimerization of Ask1 and Its Reduction by Thioredoxin-1 Regulate H₂O₂-induced c-Jun NH₂-terminal Kinase Activation and Apoptosis