The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Cellular FLICE-inhibitory Protein Splice Variants Inhibit Different Steps of Caspase-8 Activation at the CD95 Death-inducing Signaling Complex
Open accessAbstract
Upon stimulation, CD95 (APO-1/Fas) recruits the adapter molecule FADD/MORT1, procaspase-8, and the cellular FLICE-inhibitory proteins (c-FLIP) into the death-inducing signaling complex (DISC). According to the induced proximity model, procaspase-8 is activated in the DISC in an autoproteolytic manner by two subsequent cleavage steps. c-FLIP proteins exist as a long (c-FLIP(L)) and a short (c-FLIP(S)) splice variant, both of them capable of protecting cells from death receptor-mediated apoptosis. In stably transfected BJAB cells, both c-FLIP(S) and c-FLIP(L) block procaspase-8 activation at the DISC. However, cleavage is blocked at different steps. c-FLIP(L) allows the first cleavage step of procaspase-8, leading to the generation of the p10 subunit. In contrast, c-FLIP(S) completely inhibits cleavage of procaspase-8. Interestingly, p43-c-FLIP(L) lacking the p12 subunit also prevents cleavage of procaspase-8. In contrast, a nonprocessable mutant of c-FLIP(L) allows the first cleavage of procaspase-8. In conclusion, both c-FLIP proteins prevent caspase-8 activation at different levels of procaspase-8 processing at the DISC. Our results indicate that c-FLIP(L) induces a conformation of procaspase-8 that allows partial but not complete proteolytical processing, whereas in contrast c-FLIP(S) even prevents partial procaspase-8 activation at the DISC.
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Cites
1 retracted
RETRACTED: Autoimmunity as a Consequence of Retrovirus-Mediated Expression of C-FLIP in Lymphocytes
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Self-citationTwo CD95 (APO‐1/Fas) signaling pathways
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Self-citationInhibition of death receptor signals by cellular FLIP
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Self-citationCD95's deadly mission in the immune system
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Self-citationMonoclonal Antibody-Mediated Tumor Regression by Induction of Apoptosis
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Cited by
The CD95(APO-1/Fas) DISC and beyond
Peter, M. E., & Krammer, P. H. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401186 · Cited by 1,080
Self-citationChang, L., Kamata, H., Solinas, G., Luo, J.-L., Maeda, S., Venuprasad, K., Liu, Y.-C., & Karin, M. (2006) · Cell · doi:10.1016/j.cell.2006.01.021 · Cited by 706
Exploring the TRAILs less travelled: TRAIL in cancer biology and therapy
von Karstedt, S., Montinaro, A., & Walczak, H. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.28 · Cited by 556
Death receptor signal transducers: nodes of coordination in immune signaling networks
Wilson, N. S., Dixit, V., & Ashkenazi, A. (2009) · Nature Immunology · doi:10.1038/ni.1714 · Cited by 559
FLICE-Inhibitory Proteins: Regulators of Death Receptor-Mediated Apoptosis
Krueger, A., Baumann, S., Krammer, P. H., & Kirchhoff, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8247-8254.2001 · Cited by 549
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Metadata
- Authors
- Krueger, A., Schmitz, I., Baumann, S., Krammer, P. H., & Kirchhoff, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 23
- Pages
- 20633-20640
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1993327789
- Cited by
- 566
- References
- 42
- FWCI
- 10.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
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