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Fas-associated death domain protein (FADD) and caspase-8 mediate up-regulation of c-Fos by Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a FLICE inhibitory protein (FLIP)-regulated pathway.
J Biol Chem. 2001 Aug 31; 276(35):32585-90.JB

Abstract

Fas, a death domain-containing member of the tumor necrosis factor receptor family and its ligand FasL have been predominantly studied with respect to their capability to induce cell death. However, a few studies indicate a proliferation-inducing signaling activity of these molecules too. We describe here a novel signaling pathway of FasL and the tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) that triggers transcriptional activation of the proto-oncogene c-fos, a typical target gene of mitogenic pathways. FasL- and TRAIL-mediated up-regulation of c-Fos was completely dependent on the presence of Fas-associated death domain protein (FADD) and caspase-8, but caspase activity seemed to be dispensable as a pan inhibitor of caspases had no inhibitory effect. Upon overexpression of the long splice form of cellular FADD-like interleukin-1-converting enzyme (FLICE) inhibitory protein (cFLIP) in Jurkat cells, FasL- and TRAIL-induced up-regulation of c-Fos was almost completely blocked. The short splice form of FLIP, however, showed a rather stimulatory effect on c-Fos induction. Together these data demonstrate the existence of a death receptor-induced, FADD- and caspase-8-dependent pathway leading to c-Fos induction that is inhibited by the long splice form FLIP-L.

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Authors+Show Affiliations

Siegmund D
Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
Mauri D
No affiliation info available
Peters N
No affiliation info available
Juo P
No affiliation info available
Thome M
No affiliation info available
Reichwein M
No affiliation info available
Blenis J
No affiliation info available
Scheurich P
No affiliation info available
Tschopp J
No affiliation info available
Wajant H
No affiliation info available

MeSH

Adaptor Proteins, Signal TransducingAlternative SplicingAntibodies, MonoclonalApoptosisApoptosis Regulatory ProteinsCASP8 and FADD-Like Apoptosis Regulating ProteinCarrier ProteinsCaspase 8Caspase 9CaspasesFas Ligand ProteinFas-Associated Death Domain ProteinGene Expression RegulationGenes, fosHumansIntracellular Signaling Peptides and ProteinsJurkat CellsMembrane GlycoproteinsModels, BiologicalProto-Oncogene Proteins c-fosRecombinant ProteinsTNF-Related Apoptosis-Inducing LigandTransfectionTumor Necrosis Factor-alphafas Receptor

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11384965

Citation

Siegmund, D, et al. "Fas-associated Death Domain Protein (FADD) and Caspase-8 Mediate Up-regulation of c-Fos By Fas Ligand and Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) Via a FLICE Inhibitory Protein (FLIP)-regulated Pathway." The Journal of Biological Chemistry, vol. 276, no. 35, 2001, pp. 32585-90.
Siegmund D, Mauri D, Peters N, et al. Fas-associated death domain protein (FADD) and caspase-8 mediate up-regulation of c-Fos by Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a FLICE inhibitory protein (FLIP)-regulated pathway. J Biol Chem. 2001;276(35):32585-90.
Siegmund, D., Mauri, D., Peters, N., Juo, P., Thome, M., Reichwein, M., Blenis, J., Scheurich, P., Tschopp, J., & Wajant, H. (2001). Fas-associated death domain protein (FADD) and caspase-8 mediate up-regulation of c-Fos by Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a FLICE inhibitory protein (FLIP)-regulated pathway. The Journal of Biological Chemistry, 276(35), 32585-90.
Siegmund D, et al. Fas-associated Death Domain Protein (FADD) and Caspase-8 Mediate Up-regulation of c-Fos By Fas Ligand and Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) Via a FLICE Inhibitory Protein (FLIP)-regulated Pathway. J Biol Chem. 2001 Aug 31;276(35):32585-90. PubMed PMID: 11384965.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Fas-associated death domain protein (FADD) and caspase-8 mediate up-regulation of c-Fos by Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a FLICE inhibitory protein (FLIP)-regulated pathway. AU - Siegmund,D, AU - Mauri,D, AU - Peters,N, AU - Juo,P, AU - Thome,M, AU - Reichwein,M, AU - Blenis,J, AU - Scheurich,P, AU - Tschopp,J, AU - Wajant,H, Y1 - 2001/05/30/ PY - 2001/6/1/pubmed PY - 2001/10/19/medline PY - 2001/6/1/entrez SP - 32585 EP - 90 JF - The Journal of biological chemistry JO - J Biol Chem VL - 276 IS - 35 N2 - Fas, a death domain-containing member of the tumor necrosis factor receptor family and its ligand FasL have been predominantly studied with respect to their capability to induce cell death. However, a few studies indicate a proliferation-inducing signaling activity of these molecules too. We describe here a novel signaling pathway of FasL and the tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) that triggers transcriptional activation of the proto-oncogene c-fos, a typical target gene of mitogenic pathways. FasL- and TRAIL-mediated up-regulation of c-Fos was completely dependent on the presence of Fas-associated death domain protein (FADD) and caspase-8, but caspase activity seemed to be dispensable as a pan inhibitor of caspases had no inhibitory effect. Upon overexpression of the long splice form of cellular FADD-like interleukin-1-converting enzyme (FLICE) inhibitory protein (cFLIP) in Jurkat cells, FasL- and TRAIL-induced up-regulation of c-Fos was almost completely blocked. The short splice form of FLIP, however, showed a rather stimulatory effect on c-Fos induction. Together these data demonstrate the existence of a death receptor-induced, FADD- and caspase-8-dependent pathway leading to c-Fos induction that is inhibited by the long splice form FLIP-L. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/11384965/Fas_associated_death_domain_protein__FADD__and_caspase_8_mediate_up_regulation_of_c_Fos_by_Fas_ligand_and_tumor_necrosis_factor_related_apoptosis_inducing_ligand__TRAIL__via_a_FLICE_inhibitory_protein__FLIP__regulated_pathway_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)77778-1 DB - PRIME DP - Unbound Medicine ER -