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Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) (Apo2 ligand [Apo2L]) is a member of the TNF superfamily and has been shown to have selective antitumor activity. Although it is known that TRAIL (Apo2L) induces apoptosis and activates NF-kappaB and Jun N-terminal kinase (JNK) through receptors such as TRAIL-R1 (DR4) and TRAIL-R2 (DR5), the components of its signaling cascade have not been well defined. In this report, we demonstrated that the death domain kinase RIP is essential for TRAIL-induced IkappaB kinase (IKK) and JNK activation. We found that ectopic expression of the dominant negative mutant RIP, RIP(559-671), blocks TRAIL-induced IKK and JNK activation. In the RIP null fibroblasts, TRAIL failed to activate IKK and only partially activated JNK. The endogenous RIP protein was detected by immunoprecipitation in the TRAIL-R1 complex after TRAIL treatment. More importantly, we found that RIP is not involved in TRAIL-induced apoptosis. In addition, we also demonstrated that the TNF receptor-associated factor 2 (TRAF2) plays little role in TRAIL-induced IKK activation although it is required for TRAIL-mediated JNK activation. These results indicated that the death domain kinase RIP, a key factor in TNF signaling, also plays a pivotal role in TRAIL-induced IKK and JNK activation.

Titel:	The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IkappaB kinase and c-Jun N-terminal kinase.
Autor/in / Beteiligte Person:	Lin, Y ; Devin, A ; Cook, A ; Keane, MM ; Kelliher, M ; Lipkowitz, S ; Liu, ZG
Link:	Full Text Finder (Volltext)
Zeitschrift:	Molecular and cellular biology, Jg. 20 (2000-09-01), Heft 18, S. 6638-45
Veröffentlichung:	2023- : [Philadelphia] : Taylor & Francis ; <i>Original Publication</i>: [Washington, D.C.] : American Society for Microbiology, [c1981-, 2000
Medientyp:	academicJournal
ISSN:	0270-7306 (print)
DOI:	10.1128/MCB.20.18.6638-6645.2000
Schlagwort:	Animals Apoptosis Regulatory Proteins Cell Line Enzyme Activation Fibroblasts cytology HeLa Cells Humans I-kappa B Kinase JNK Mitogen-Activated Protein Kinases Ligands Membrane Glycoproteins genetics Mice Mutagenesis Protein Serine-Threonine Kinases genetics Proteins genetics Proteins physiology Receptor-Interacting Protein Serine-Threonine Kinases Receptors, TNF-Related Apoptosis-Inducing Ligand Receptors, Tumor Necrosis Factor metabolism Recombinant Fusion Proteins genetics Recombinant Fusion Proteins metabolism Signal Transduction TNF Receptor-Associated Factor 2 TNF-Related Apoptosis-Inducing Ligand Tumor Necrosis Factor-alpha genetics Apoptosis Membrane Glycoproteins metabolism Mitogen-Activated Protein Kinases metabolism Protein Serine-Threonine Kinases metabolism Proteins metabolism Tumor Necrosis Factor-alpha metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article Language: English [Mol Cell Biol] 2000 Sep; Vol. 20 (18), pp. 6638-45. MeSH Terms: Apoptosis* ; Membrane Glycoproteins / metabolism ; Mitogen-Activated Protein Kinases / metabolism ; Protein Serine-Threonine Kinases / metabolism ; Proteins / metabolism ; Tumor Necrosis Factor-alpha / *metabolism ; Animals ; Apoptosis Regulatory Proteins ; Cell Line ; Enzyme Activation ; Fibroblasts / cytology ; HeLa Cells ; Humans ; I-kappa B Kinase ; JNK Mitogen-Activated Protein Kinases ; Ligands ; Membrane Glycoproteins / genetics ; Mice ; Mutagenesis ; Protein Serine-Threonine Kinases / genetics ; Proteins / genetics ; Proteins / physiology ; Receptor-Interacting Protein Serine-Threonine Kinases ; Receptors, TNF-Related Apoptosis-Inducing Ligand ; Receptors, Tumor Necrosis Factor / metabolism ; Recombinant Fusion Proteins / genetics ; Recombinant Fusion Proteins / metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 2 ; TNF-Related Apoptosis-Inducing Ligand ; Tumor Necrosis Factor-alpha / genetics References: Science. 1997 Oct 31;278(5339):860-6. 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(PMID: 9721089) Grant Information: R01 GM061298 United States GM NIGMS NIH HHS Substance Nomenclature: 0 (Apoptosis Regulatory Proteins) ; 0 (Ligands) ; 0 (Membrane Glycoproteins) ; 0 (Proteins) ; 0 (Receptors, TNF-Related Apoptosis-Inducing Ligand) ; 0 (Receptors, Tumor Necrosis Factor) ; 0 (Recombinant Fusion Proteins) ; 0 (TNF Receptor-Associated Factor 2) ; 0 (TNF-Related Apoptosis-Inducing Ligand) ; 0 (TNFRSF10A protein, human) ; 0 (TNFSF10 protein, human) ; 0 (Tnfsf10 protein, mouse) ; 0 (Tumor Necrosis Factor-alpha) ; EC 2.7.11.1 (Protein Serine-Threonine Kinases) ; EC 2.7.11.1 (RIPK1 protein, human) ; EC 2.7.11.1 (Receptor-Interacting Protein Serine-Threonine Kinases) ; EC 2.7.11.1 (Ripk1 protein, mouse) ; EC 2.7.11.10 (CHUK protein, human) ; EC 2.7.11.10 (Chuk protein, mouse) ; EC 2.7.11.10 (I-kappa B Kinase) ; EC 2.7.11.10 (IKBKB protein, human) ; EC 2.7.11.10 (IKBKE protein, human) ; EC 2.7.11.10 (Ikbkb protein, mouse) ; EC 2.7.11.10 (Ikbke protein, mouse) ; EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases) ; EC 2.7.11.24 (Mitogen-Activated Protein Kinases) Entry Date(s): Date Created: 20000825 Date Completed: 20000922 Latest Revision: 20220331 Update Code: 20240513 PubMed Central ID: PMC86162

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The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IkappaB kinase and c-Jun N-terminal kinase.