Academic Journal
Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-κB Activation and Cell Survival.
| العنوان: | Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-κB Activation and Cell Survival. |
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| المؤلفون: | Horn, S, Hughes, MA, Schilling, R, Sticht, C, Tenev, T, Ploesser, M, Meier, P, Sprick, MR, MacFarlane, M, Leverkus, M |
| بيانات النشر: | Elsevier |
| سنة النشر: | 2019 |
| المجموعة: | University of Leicester: Leicester Research Archive (LRA) |
| مصطلحات موضوعية: | CD95, DISC, NF-κB, cFLIP, caspase-10, caspase-8, cell death, Apoptosis, CASP8 and FADD-Like Apoptosis Regulating Protein, Caspase 10, Caspase 8, Cell Line, Cell Survival, Clustered Regularly Interspaced Short Palindromic Repeats, Fas Ligand Protein, Fas-Associated Death Domain Protein, HeLa Cells, Humans, Imidazoles, Indoles, Interleukin-8, NF-KappaB Inhibitor alpha, NF-kappa B, Oligopeptides, RNA Interference, RNA, Messenger, Small Interfering, Signal Transduction, fas Receptor |
| الوصف: | The accession number for the microarray dataset reported in this paper is GEO: GSE75365. Supplementary information is available to download from the publisher's website at https://doi.org/10.1016/j.celrep.2017.04.010 ; Formation of the death-inducing signaling complex (DISC) initiates extrinsic apoptosis. Caspase-8 and its regulator cFLIP control death signaling by binding to death-receptor-bound FADD. By elucidating the function of the caspase-8 homolog, caspase-10, we discover that caspase-10 negatively regulates caspase-8-mediated cell death. Significantly, we reveal that caspase-10 reduces DISC association and activation of caspase-8. Furthermore, we extend our co-operative/hierarchical binding model of caspase-8/cFLIP and show that caspase-10 does not compete with caspase-8 for binding to FADD. Utilizing caspase-8-knockout cells, we demonstrate that caspase-8 is required upstream of both cFLIP and caspase-10 and that DISC formation critically depends on the scaffold function of caspase-8. We establish that caspase-10 rewires DISC signaling to NF-κB activation/cell survival and demonstrate that the catalytic activity of caspase-10, and caspase-8, is redundant in gene induction. Thus, our data are consistent with a model in which both caspase-10 and cFLIP coordinately regulate CD95L-mediated signaling for death or survival. ; Work in the laboratory of M.L. was funded by EU Horizon 2020 (MelPlex ESR network; project 5) and grants of the Deutsche Forschungsgemeinschaft (Le 953/6-1 and 953/8-1). M.L. was supported by Deutsche Forschungsgemeinschaft RTG 2099 (projects 9 and 10). Project 9 supports R.S., and project 10 provides funding for S.H. M.R.S. is supported by the Dietmar Hopp Foundation. M.M. and M.A.H. are supported by the UK Medical Research Council. ; Peer-reviewed ; Publisher Version |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 2211-1247 |
| Relation: | https://www.ncbi.nlm.nih.gov/pubmed/28445729; Cell Reports, 19 (4), pp. 785-797; http://hdl.handle.net/2381/44860 |
| DOI: | 10.1016/j.celrep.2017.04.010 |
| الاتاحة: | http://hdl.handle.net/2381/44860 https://doi.org/10.1016/j.celrep.2017.04.010 |
| Rights: | Copyright © the authors, 2017. This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
| رقم الانضمام: | edsbas.C490C205 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 22111247 |
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| DOI: | 10.1016/j.celrep.2017.04.010 |