The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-κB and MAPK signaling
Open accessAbstract
Significance: Pathogenic organisms express virulence factors that can inhibit immune signaling pathways. Thus, the immune system is faced with the challenge of eliciting an effective inflammatory response to pathogens that actively suppress inflammation. The mechanisms that regulate this response are largely undefined. The Yersinia virulence factor YopJ blocks NF-κB and MAPK signaling, resulting in reduced cytokine production and target cell death. Here, we find that caspase-8, RIPK1, and FADD are required for YopJ-induced cell death and show that mice lacking caspase-8 are severely susceptible to Yersinia infection and have defective proinflammatory cytokine production. These findings highlight a possible mechanism of immune defense that can overcome pathogen inhibition of cell-intrinsic proinflammatory immune responses.
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Citations
Cites
Recognition of microorganisms and activation of the immune response
Medzhitov, R. (2007) · Nature · doi:10.1038/nature06246 · Cited by 2,862
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059
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 · cited 2×
“Caspase-8 catalytic activity prevents a lethal RIPK3-dependent programmed necrosis that occurs in early embryonic development (23).”
BackgroundSelf-citationInhibitor of Apoptosis Proteins Limit RIP3 Kinase-Dependent Interleukin-1 Activation
Vince, J. E., Wong, W. W.-L., Gentle, I., Lawlor, K. E., Allam, R., O'Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.012 · Cited by 491
The Role of the Kinases RIP1 and RIP3 in TNF-Induced Necrosis
Vandenabeele, P., Declercq, W., Van Herreweghe, F., & Vanden Berghe, T. (2010) · Science Signaling · doi:10.1126/scisignal.3115re4 · Cited by 482
Survival Function of the FADD-CASPASE-8-cFLIPL Complex
Dillon, C. P., Oberst, A., Weinlich, R., Janke, L. J., Kang, T.-B., Ben-Moshe, T., Mak, T. W., Wallach, D., & Green, D. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.010 · Cited by 331 · cited 1×
“Fadd mice exhibit embryonic lethality that is reverted with loss of RIPK3 (29).”
BackgroundSelf-citationEssential Role for Caspase-8 in Toll-like Receptors and NFκB Signaling
Lemmers, B., Salmena, L., Bidère, N., Su, H., Matysiak-Zablocki, E., Murakami, K., Ohashi, P. S., Jurisicova, A., Lenardo, M., Hakem, R., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606721200 · Cited by 181
Koenig, A., Buskiewicz, I. A., Fortner, K. A., Russell, J. Q., Asaoka, T., He, Y.-W., Hakem, R., Eriksson, J. E., & Budd, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506428 · Cited by 42
Cited by
Necroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148
Necroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016
Self-citationGenetic Mechanisms of Immune Evasion in Colorectal Cancer
Grasso, C. S., Giannakis, M., Wells, D. K., Hamada, T., Mu, X. J., Quist, M., Nowak, J. A., Nishihara, R., Qian, Z. R., Inamura, K., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-1327 · Cited by 535
“Four additional significantly mutated immune-related genes had been previously described as being expressed in cancer cells: CD58, a tumor surface protein involved in the activation of NK cells through interaction with CD2 (29) that is concurrently lost with B2M in some cancers (30); CASP8, a tumor-expressed gene invo…”
BackgroundSamir, P., Malireddi, R. K. S., & Kanneganti, T.-D. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00238 · Cited by 557
Wang, Y., & Kanneganti, T.-D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.038 · Cited by 545
Metadata
- Authors
- Philip, N. H., Dillon, C. P., Snyder, A. G., Fitzgerald, P., Wynosky-Dolfi, M. A., Zwack, E. E., Hu, B., Fitzgerald, L., Mauldin, E. A., Copenhaver, A. M., Shin, S., Wei, L., Parker, M., Zhang, J., Oberst, A., Green, D. R., & Brodsky, I. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-05-05
- Volume
- 111
- Issue
- 20
- Pages
- 7385-7390
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2073678899
- Cited by
- 280
- References
- 8
- FWCI
- 9.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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- The paper
- Philip, N. H., Dillon, C. P., Snyder, A. G., Fitzgerald, P., Wynosky-Dolfi, M. A., Zwack, E. E., Hu, B., Fitzgerald, L., Mauldin, E. A., Copenhaver, A. M., Shin, S., Wei, L., Parker, M., Zhang, J., Oberst, A., Green, D. R., & Brodsky, I. E. (2014). Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-κB and MAPK signaling. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1403252111
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
