The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Activation of caspases-8 and -10 by FLIPL
Open accessAbstract
The first step in caspase activation is transition of the latent zymogen to an active form. For the initiator caspases, this occurs through dimerization of monomeric zymogens at an activating complex. Recent studies have suggested that FLIPL [FLICE-like inhibitory protein, long form; FLICE is FADD (Fas-associated death domain protein)-like interleukin-1β-converting enzyme], previously thought to act solely as an inhibitor of caspase-8 activation, can under certain circumstances function to enhance caspase activation. Using an in vitro induced-proximity assay, we demonstrate that activation of caspases-8 and -10 occurs independently of cleavage of either the caspase or FLIPL. FLIPL activates caspase-8 by forming heterodimeric enzyme molecules with substrate specificity and catalytic activity indistinguishable from those of caspase-8 homodimers. Significantly, the barrier for heterodimer formation is lower than that for homodimer formation, suggesting that FLIPL is a more potent activator of caspase-8 than is caspase-8 itself.
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Citations
Cites
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Cited by
Caspase Functions in Cell Death and Disease
McIlwain, D. R., Berger, T., & Mak, T. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008656 · Cited by 2,594
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278
“Biochemical and structural studies have indicated that FLIP can heterodimerize with caspase-8 in kosmotropic salt, and that this complex may be able to impart catalytic activity on caspase-8 in the absence of interdomain cleavage18,19.”
Self-citationThe many roles of FAS receptor signaling in the immune system
Strasser, A., Jost, P. J., & Nagata, S. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.001 · Cited by 968
Jin, Z., Li, Y., Pitti, R., Lawrence, D., Pham, V. C., Lill, J. R., & Ashkenazi, A. (2009) · Cell · doi:10.1016/j.cell.2009.03.015 · Cited by 591
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
Metadata
- Authors
- BOATRIGHT, K. M., DEIS, C., DENAULT, J.-B., SUTHERLIN, D. P., & SALVESEN, G. S.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2004-08-24
- Volume
- 382
- Issue
- 2
- Pages
- 651-657
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2059444339
- Cited by
- 245
- References
- 1
- FWCI
- 6.34
- Type
- journal article
- Language
- en
- Open access
- green
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- BOATRIGHT, K. M., DEIS, C., DENAULT, J.-B., SUTHERLIN, D. P., & SALVESEN, G. S. (2004). Activation of caspases-8 and -10 by FLIPL. Biochemical Journal. https://doi.org/10.1042/bj20040809
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