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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.

Authors+Show Affiliations

Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

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 -