Letai, A. Cell death and cancer therapy: don’t forget to kill the cancer cell! Clin. Cancer Res. 21, 5015–5020 (2015).
Roberts, A. W. et al. Targeting BCL2 with venetoclax in relapsed chronic lymphocytic leukemia. N. Engl. J. Med. 374, 311–322 (2016).
Marin-Acevedo, J. A., Soyano, A. E., Dholaria, B., Knutson, K. L. & Lou, Y. Cancer immunotherapy beyond immune checkpoint inhibitors. J. Hematol. Oncol. 11, 8 (2018).
Vasan, N., Baselga, J. & Hyman, D. M. A view on drug resistance in cancer. Nature 575, 299–309 (2019).
Hangauer, M. J. et al. Drug-tolerant persister cancer cells are vulnerable to GPX4 inhibition. Nature 551, 247–250 (2017).
Cabanos, H. F. & Hata, A. N. Emerging insights into targeted therapy-tolerant persister cells in cancer. Cancers 13, 2666 (2021).
Pfeffer, C. M. & Singh, A. T. K. Apoptosis: a target for anticancer therapy. Int. J. Mol. Sci. 19, 448 (2018).
Legrand, A. J., Konstantinou, M., Goode, E. F. & Meier, P. The diversification of cell death and immunity: memento mori. Mol. Cell 76, 232–242 (2019).
Fadok, V. A. et al. Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF. J. Clin. Invest. 101, 890–898 (1998).
Voll, R. E. et al. Immunosuppressive effects of apoptotic cells. Nature 390, 350–351 (1997).
Vitale, I. et al. Apoptotic cell death in disease — current understanding of the NCCD 2023. Cell Death Differ. 30, 1097–1154 (2023).
Segawa, K. & Nagata, S. An apoptotic ‘eat me’ signal: phosphatidylserine exposure. Trends Cell Biol. 25, 639–650 (2015).
Scaffidi, C., Schmitz, I., Krammer, P. H. & Peter, M. E. The role of c-FLIP in modulation of CD95-induced apoptosis. J. Biol. Chem. 274, 1541 (1999).
Pasparakis, M. & Vandenabeele, P. Necroptosis and its role in inflammation. Nature 517, 311–320 (2015).
Fulda, S. Therapeutic exploitation of necroptosis for cancer therapy. Semin. Cell Dev. Biol. 35, 51–56 (2014).
Su, Z., Yang, Z., Xu, Y., Chen, Y. & Yu, Q. Apoptosis, autophagy, necroptosis, and cancer metastasis. Mol. Cancer 14, 48 (2015).
Nicolai, S., Pieraccioli, M., Peschiaroli, A., Melino, G. & Raschella, G. Neuroblastoma: oncogenic mechanisms and therapeutic exploitation of necroptosis. Cell Death Dis. 6, e2010 (2015).
Moriwaki, K. & Chan, F. K. Regulation of RIPK3- and RHIM-dependent necroptosis by the proteasome. J. Biol. Chem. 291, 5948–5959 (2016).
Kaczmarek, A., Vandenabeele, P. & Krysko, D. V. Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity 38, 209–223 (2013).
Brault, M., Olsen, T. M., Martinez, J., Stetson, D. B. & Oberst, A. Intracellular nucleic acid sensing triggers necroptosis through synergistic type I IFN and TNF signaling. J. Immunol. 200, 2748–2756 (2018).
Hildebrand, J. M. et al. Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death. Proc. Natl Acad. Sci. USA 111, 15072–15077 (2014).
Chen, X. et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 24, 105–121 (2014).
Cai, Z. et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat. Cell Biol. 16, 55–65 (2014).
Murphy, J. M. et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443–453 (2013).
Meng, Y. et al. Human RIPK3 C-lobe phosphorylation is essential for necroptotic signaling. Cell Death Dis. 13, 565 (2022).
Vanden Berghe, T., Hassannia, B. & Vandenabeele, P. An outline of necrosome triggers. Cell. Mol. Life Sci. 73, 2137–2152 (2016).
Vercammen, D. et al. Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J. Exp. Med. 188, 919–930 (1998).
Vercammen, D. et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J. Exp. Med. 187, 1477–1485 (1998).
Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1, 489–495 (2000). In this seminal paper, the first identification of RIPK1 as an essential mediator of necroptosis is provided.
Ermolaeva, M. A. et al. Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nat. Immunol. 9, 1037–1046 (2008).
Pobezinskaya, Y. L. et al. The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors. Nat. Immunol. 9, 1047–1054 (2008).
Micheau, O. & Tschopp, J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181–190 (2003). The groundbreaking first description of the TNFR1 complex I and complex II.
Hsu, H., Xiong, J. & Goeddel, D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 81, 495–504 (1995).
Rothe, M. et al. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83, 1243–1252 (1995).
Shu, H. B., Takeuchi, M. & Goeddel, D. V. The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. Proc. Natl Acad. Sci. USA 93, 13973–13978 (1996).
Varfolomeev, E. et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor α (TNFα)-induced NF-κB activation. J. Biol. Chem. 283, 24295–24299 (2008).
Lafont, E. et al. TBK1 and IKKepsilon prevent TNF-induced cell death by RIPK1 phosphorylation. Nat. Cell Biol. 20, 1389–1399 (2018).
Xu, D. et al. TBK1 suppresses RIPK1-driven apoptosis and inflammation during development and in aging. Cell 174, 1477–1491.e19 (2018).
Haas, K. F., Miller, S. L., Friedman, D. B. & Broadie, K. The ubiquitin-proteasome system postsynaptically regulates glutamatergic synaptic function. Mol. Cell. Neurosci. 35, 64–75 (2007).
Jaco, I. et al. MK2 phosphorylates RIPK1 to prevent TNF-induced cell death. Mol. Cell 66, 698–710.e5 (2017).
Dondelinger, Y. et al. MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death. Nat. Cell Biol. 19, 1237–1247 (2017).
Menon, M. B. et al. p38MAPK/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection. Nat. Cell Biol. 19, 1248–1259 (2017).
Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591–596 (2011).
Dynek, J. N. et al. c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J. 29, 4198–4209 (2010).
Bertrand, M. J. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689–700 (2008).
Ea, C. K., Deng, L., Xia, Z. P., Pineda, G. & Chen, Z. J. Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245–257 (2006).
留言 (0)