共查询到20条相似文献,搜索用时 15 毫秒
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William J. Kaiser Haripriya Sridharan Chunzi Huang Pratyusha Mandal Jason W. Upton Peter J. Gough Clark A. Sehon Robert W. Marquis John Bertin Edward S. Mocarski 《The Journal of biological chemistry》2013,288(43):31268-31279
Toll-like receptor (TLR) signaling is triggered by pathogen-associated molecular patterns that mediate well established cytokine-driven pathways, activating NF-κB together with IRF3/IRF7. In addition, TLR3 drives caspase 8-regulated programmed cell death pathways reminiscent of TNF family death receptor signaling. We find that inhibition or elimination of caspase 8 during stimulation of TLR2, TLR3, TLR4, TLR5, or TLR9 results in receptor interacting protein (RIP) 3 kinase-dependent programmed necrosis that occurs through either TIR domain-containing adapter-inducing interferon-β (TRIF) or MyD88 signal transduction. TLR3 or TLR4 directly activates programmed necrosis through a RIP homotypic interaction motif-dependent association of TRIF with RIP3 kinase (also called RIPK3). In fibroblasts, this pathway proceeds independent of RIP1 or its kinase activity, but it remains dependent on mixed lineage kinase domain-like protein (MLKL) downstream of RIP3 kinase. Here, we describe two small molecule RIP3 kinase inhibitors and employ them to demonstrate the common requirement for RIP3 kinase in programmed necrosis induced by RIP1-RIP3, DAI-RIP3, and TRIF-RIP3 complexes. Cell fate decisions following TLR signaling parallel death receptor signaling and rely on caspase 8 to suppress RIP3-dependent programmed necrosis whether initiated directly by a TRIF-RIP3-MLKL pathway or indirectly via TNF activation and the RIP1-RIP3-MLKL necroptosis pathway. 相似文献
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Ruiz-Ruiz C Ruiz de Almodóvar C Rodríguez A Ortiz-Ferrón G Redondo JM López-Rivas A 《The Journal of biological chemistry》2004,279(19):19712-19720
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Meraro D Gleit-Kielmanowicz M Hauser H Levi BZ 《Journal of immunology (Baltimore, Md. : 1950)》2002,168(12):6224-6231
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Lefebvre S Berrih-Aknin S Adrian F Moreau P Poea S Gourand L Dausset J Carosella ED Paul P 《The Journal of biological chemistry》2001,276(9):6133-6139
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Francis McCoy Rashid Darbandi Si-Ing Chen Laura Eckard Keela Dodd Kelly Jones Anthony J. Baucum II Jennifer A. Gibbons Sue-Hwa Lin Roger J. Colbran Leta K. Nutt 《The Journal of biological chemistry》2013,288(13):8838-8848
The metabolism of the Xenopus laevis egg provides a cell survival signal. We found previously that increased carbon flux from glucose-6-phosphate (G6P) through the pentose phosphate pathway in egg extracts maintains NADPH levels and calcium/calmodulin regulated protein kinase II (CaMKII) activity to phosphorylate caspase 2 and suppress cell death pathways. Here we show that the addition of G6P to oocyte extracts inhibits the dephosphorylation/inactivation of CaMKII bound to caspase 2 by protein phosphatase 1. Thus, G6P sustains the phosphorylation of caspase 2 by CaMKII at Ser-135, preventing the induction of caspase 2-mediated apoptotic pathways. These findings expand our understanding of oocyte biology and clarify mechanisms underlying the metabolic regulation of CaMKII and apoptosis. Furthermore, these findings suggest novel approaches to disrupt the suppressive effects of the abnormal metabolism on cell death pathways. 相似文献
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Gamma interferon triggers interaction between ICSBP (IRF-8) and TEL,recruiting the histone deacetylase HDAC3 to the interferon-responsive element 下载免费PDF全文
Kuwata T Gongora C Kanno Y Sakaguchi K Tamura T Kanno T Basrur V Martinez R Appella E Golub T Ozato K 《Molecular and cellular biology》2002,22(21):7439-7448
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Iyo Matsuda Kentaro Matsuo Yuka Matsushita Yasushi Haruna Masamitsu Niwa Takao Kataoka 《The Journal of biological chemistry》2014,289(7):3876-3887
Caspase 8 plays an essential role in the regulation of apoptotic and non-apoptotic signaling pathways. The long form of cellular FLICE-inhibitory protein (c-FLIPL) has been shown previously to regulate caspase 8-dependent nuclear factor κB (NF-κB) activation by receptor-interacting protein 1 (RIP1) and TNF receptor-associated factor 2 (TRAF2). In this study, the molecular mechanism by which c-FLIPL regulates caspase 8-dependent NF-κB activation was further explored in the human embryonic kidney cell line HEK 293 and variant cells barely expressing caspase 8. The caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone greatly diminished caspase 8-dependent NF-κB activation induced by Fas ligand (FasL) when c-FLIPL, but not its N-terminal fragment c-FLIP(p43), was expressed. The prodomain of caspase 8 was found to interact with the RIP1 death domain and to be sufficient to mediate NF-κB activation induced by FasL or c-FLIP(p43). The interaction of the RIP1 death domain with caspase 8 was inhibited by c-FLIPL but not c-FLIP(p43). Thus, these results reveal that the C-terminal domain of c-FLIPL specifically inhibits the interaction of the caspase 8 prodomain with the RIP1 death domain and, thereby, regulates caspase 8-dependent NF-κB activation. 相似文献
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Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain 下载免费PDF全文
Miyamoto S Suzuki T Muto S Aizawa K Kimura A Mizuno Y Nagino T Imai Y Adachi N Horikoshi M Nagai R 《Molecular and cellular biology》2003,23(23):8528-8541