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Enregistrement W2012440244 · doi:10.1074/jbc.c000917200

Stress-induced Inhibition of ERK1 and ERK2 by Direct Interaction with p38 MAP Kinase

2001· article· en· W2012440244 sur OpenAlex

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Notice bibliographique

RevueJournal of Biological Chemistry · 2001
Typearticle
Langueen
DomaineBiochemistry, Genetics and Molecular Biology
ThématiqueMelanoma and MAPK Pathways
Établissements canadiensKinexus Bioinformatics Corporation (Canada)University of British Columbia
Organismes subventionnairesnon disponible
Mots-clésASK1Mitogen-activated protein kinase kinaseMAP2K7MAP kinase kinase kinaseMAPK14KinaseProtein kinase Ac-RafMitogen-activated protein kinaseCyclin-dependent kinase 9MAPK/ERK pathwayp38 mitogen-activated protein kinasesPhosphorylationActivator (genetics)Cyclin-dependent kinase 2Molecular biologyCell biologyBiologyChemistryBiochemistry

Résumé

récupéré en direct d'OpenAlex

We have identified a direct physical interaction between the stress signaling p38α MAP kinase and the mitogen-activated protein kinases ERK1 and ERK2 by affinity chromatography and coimmunoprecipitation studies. Phosphorylation and activation of p38α enhanced its interaction with ERK1/2, and this correlated with inhibition of ERK1/2 phosphotransferase activity. The loss of epidermal growth factor-induced activation and phosphorylation of ERK1/2 but not of their direct activator MEK1 in HeLa cells transfected with the p38α activator MKK6(E) indicated that activated p38α may sequester ERK1/2 and sterically block their phosphorylation by MEK1. We have identified a direct physical interaction between the stress signaling p38α MAP kinase and the mitogen-activated protein kinases ERK1 and ERK2 by affinity chromatography and coimmunoprecipitation studies. Phosphorylation and activation of p38α enhanced its interaction with ERK1/2, and this correlated with inhibition of ERK1/2 phosphotransferase activity. The loss of epidermal growth factor-induced activation and phosphorylation of ERK1/2 but not of their direct activator MEK1 in HeLa cells transfected with the p38α activator MKK6(E) indicated that activated p38α may sequester ERK1/2 and sterically block their phosphorylation by MEK1. mitogen-activated protein extracellular signal-regulated kinase MAP/ERK kinase MAP kinase kinase glutathioneS-transferase polyacrylamide gel electrophoresis Dulbecco's minimum essential medium dithiothreitol myelin basic protein 3-(N-morpholino)propanesulfonic acid epidermal growth factor Mitogen-activated protein (MAP)1 kinase modules are involved in the signal transduction of a wide variety of cellular responses in all eukaryotic organisms including proliferation, differentiation, and apoptosis (1English J. Pearson G. Wilsbacher J. Swantek J. Karandikar M. Xu S. Cobb M.H. Exp. Cell Res. 1999; 253: 255-270Crossref PubMed Scopus (377) Google Scholar). At least four distinct and parallel MAP kinase cascades have been identified, including extracellular signal-regulated kinases 1 and 2 (ERK1/2), the p38 MAP kinases, c-jun N-terminal or stress-activated protein kinases (JNK/SAPK), and ERK5/big MAP kinase 1 (BMK1). It is well established that ERK1/2 are typically stimulated by growth-related stimuli through the Raf1/B-MEK1/2-ERK1/2 protein kinase cascade. The JNK and p38 MAP kinases are primarily activated by stress-related signals such as heat and osmotic shock, UV irradiation, and proinflammatory cytokines by means of the MAP kinase kinases, MKK3, -4, -6, and -7 (2Ono K. Han J. Cell. Signal. 2000; 12: 1-13Crossref PubMed Scopus (1382) Google Scholar, 3Ichijo H. Oncogene. 1999; 18: 6087-6093Crossref PubMed Scopus (472) Google Scholar, 4Leppa S. Bohmann D. Oncogene. 1999; 18: 6158-6162Crossref PubMed Scopus (437) Google Scholar). Whereas the selective activation of distinct MAP kinase pathways in response to different extracellular stimuli has been extensively documented, there is increasing evidence for cross-talk between distinct MAP kinase pathways. A p38-dependent ERK1/2 activation was observed in several mammalian cell lines including the human embryonic kidney cell line HEK293 upon arsenite treatment (5Ludwig S. Hoffmeyer A. Goebeler M. Kilian K. Hafner H. Neufeld B. Han J. Rapp U.R. J. Biol. Chem. 1998; 273: 1917-1922Abstract Full Text Full Text PDF PubMed Scopus (199) Google Scholar). It was also found that inactivation of p38 by SB202190 treatment resulted in a delayed and prolonged activation of ERK1/2 in the human hepatoma cell line, HepG2 (6Singh R.P. Dhawan P. Golden C. Kapoor G.S. Mehta K.D. J. Biol. Chem. 1999; 274: 19593-19600Abstract Full Text Full Text PDF PubMed Scopus (152) Google Scholar). In both cases, MEK1 was implicated in the activation of ERK1/2. Here we report that in HeLa and HEK293 cells, stress stimuli lead to an inhibition of ERK1/2 via p38α. Phosphorylated p38α is capable of forming a complex with ERK1/2, and it prevents their phosphorylation by MEK1/2. Mitogen-activated protein (MAP)1 kinase modules are involved in the signal transduction of a wide variety of cellular responses in all eukaryotic organisms including proliferation, differentiation, and apoptosis (1English J. Pearson G. Wilsbacher J. Swantek J. Karandikar M. Xu S. Cobb M.H. Exp. Cell Res. 1999; 253: 255-270Crossref PubMed Scopus (377) Google Scholar). At least four distinct and parallel MAP kinase cascades have been identified, including extracellular signal-regulated kinases 1 and 2 (ERK1/2), the p38 MAP kinases, c-jun N-terminal or stress-activated protein kinases (JNK/SAPK), and ERK5/big MAP kinase 1 (BMK1). It is well established that ERK1/2 are typically stimulated by growth-related stimuli through the Raf1/B-MEK1/2-ERK1/2 protein kinase cascade. The JNK and p38 MAP kinases are primarily activated by stress-related signals such as heat and osmotic shock, UV irradiation, and proinflammatory cytokines by means of the MAP kinase kinases, MKK3, -4, -6, and -7 (2Ono K. Han J. Cell. Signal. 2000; 12: 1-13Crossref PubMed Scopus (1382) Google Scholar, 3Ichijo H. Oncogene. 1999; 18: 6087-6093Crossref PubMed Scopus (472) Google Scholar, 4Leppa S. Bohmann D. Oncogene. 1999; 18: 6158-6162Crossref PubMed Scopus (437) Google Scholar). Whereas the selective activation of distinct MAP kinase pathways in response to different extracellular stimuli has been extensively documented, there is increasing evidence for cross-talk between distinct MAP kinase pathways. A p38-dependent ERK1/2 activation was observed in several mammalian cell lines including the human embryonic kidney cell line HEK293 upon arsenite treatment (5Ludwig S. Hoffmeyer A. Goebeler M. Kilian K. Hafner H. Neufeld B. Han J. Rapp U.R. J. Biol. Chem. 1998; 273: 1917-1922Abstract Full Text Full Text PDF PubMed Scopus (199) Google Scholar). It was also found that inactivation of p38 by SB202190 treatment resulted in a delayed and prolonged activation of ERK1/2 in the human hepatoma cell line, HepG2 (6Singh R.P. Dhawan P. Golden C. Kapoor G.S. Mehta K.D. J. Biol. Chem. 1999; 274: 19593-19600Abstract Full Text Full Text PDF PubMed Scopus (152) Google Scholar). In both cases, MEK1 was implicated in the activation of ERK1/2. Here we report that in HeLa and HEK293 cells, stress stimuli lead to an inhibition of ERK1/2 via p38α. Phosphorylated p38α is capable of forming a complex with ERK1/2, and it prevents their phosphorylation by MEK1/2. We thank Dr. J. Han, the Scripps Research Institute (La Jolla, CA) for pcDNA3-flagp38α wild-type and p38α (AF) dominant negative mutant. Constructs of constitutively active MKK6(E) mutants, pGEX-MKK6(E) and pcDNA3-MKK6(E), were provided by Dr. C. Glembotski, San Diego State University and Dr. R. Davis, University of Massachusetts, respectively.

Récupéré en direct depuis OpenAlex et désinversé. Les résumés ne sont pas conservés dans cette base de données : les index inversés représentent 8,6 Go des 9,3 Go de texte de la base, et le serveur dispose de 13 Go libres.

Prédiction distillée sur la base complète

Imitation des enseignants

Ni prévalence calibrée, ni vérité terrain. Validation humaine à venir. Apprise à partir de 10 348 étiquettes directes de Codex et de 10 348 étiquettes directes de Gemma. Le mode candidate est l'union des têtes enseignantes seuillées; le consensus est leur intersection. Ces sorties portent le statut machine_predicted_unvalidated et ne sont ni des étiquettes humaines ni des étiquettes directes de modèles de pointe.

score de la tête « metaresearch » (Codex)0,000
score de la tête « metaresearch » (Gemma)0,000
Version: codex-gemma-dda1882f352aStatut de validation: machine_predicted_unvalidated
Catégories candidatesaucune
Catégories consensuellesaucune
DomaineSignal candidat: aucune · Signal consensuel: aucune
Devis d'étudeSignal candidat: Expérimental (laboratoire) · Signal consensuel: Expérimental (laboratoire)
GenreSignal candidat: Empirique · Signal consensuel: Empirique
Score de désaccord entre enseignants0,005
Score d'incertitude au seuil0,322

Scores Codex et Gemma par catégorie

CatégorieCodexGemma
Métarecherche0,0000,000
Méta-épidémiologie (sens strict)0,0000,000
Méta-épidémiologie (sens large)0,0000,000
Bibliométrie0,0000,000
Études des sciences et des technologies0,0000,000
Communication savante0,0000,000
Science ouverte0,0000,000
Intégrité de la recherche0,0000,000
Charge utile insuffisante (le modèle a refusé de juger)0,0000,000

Scores machine (provisoires)

Les deux têtes enseignantes du modèle étudiant, lues sur ce travail. Un score ordonne la base pour la relecture; il n'affirme jamais une catégorie, et le statut de validation accompagne chaque rangée tel quel.

Scores de référence d'un modèle non mature (critères de maturité non atteints, 7 itérations). Un score ordonne; il n'affirme jamais une catégorie.

Tête enseignante Opus0,015
Tête enseignante GPT0,238
Écart entre enseignants0,223 · la distance entre les deux têtes enseignantes sur ce seul travail
Statut de validationscore_only:v0-immature-baseline · tel quel depuis la passe de notation : score_only signifie que le nombre peut ordonner les travaux, et qu'aucune étiquette de catégorie n'en découle