cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination.
By M. Bertrand, S. Milutinovic, K. Dickson, W. Ho, A. Boudreault, J. Durkin, J. Gillard, James B. Jaquith, S. Morris, P. Barker. Molecules and Cells, 2008
1,120 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/6adf25f1f4f929a116af1890287242c115c7c98a
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Citations in the corpus
- SPHINGOSINE-1-PHOSPHATE: A MISSING COFACTOR FOR THE E3 UBIQUITIN LIGASE TRAF2 (2010, neutral): “Although TRAF2 can act as an adaptor for cIAP1 and cIAP2 that can themselves serve as E3 ligases for RIP1 21–23, neither cIAPs nor TRAF5 were associated with purified TRAF2 used for in vitro ubiquitination assays (Supplementary Fig.”
- Regulation of tumour necrosis factor signalling: live or let die (2015, background): “36 ) .”
- Caspases in Cell Death, Inflammation, and Gasdermin-Induced Pyroptosis (2020, background): “Here, cIAPs modify RIPK1 by Lys63-linked ubiquitination (1, 54, 55) to promote the scaffolding function, but not kinase activity, of RIPK1 to assemble a multiprotein signaling complex that activates prosurvival NF-κB transcriptional responses.”
- The noncanonical NF‐κB pathway (2012, background): “Moreover, cIAP1 ⁄ 2 also possess K63 type of E3 activity toward receptor interacting protein 1 (RIP1), which is important for mediating the activation of canonical NF-jB and cell survival (63, 64).”
- The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. (2011, background): “Nonetheless, SM treatment abrogates constitutive ubiquitylation of RIP1 (Bertrand et al., 2008), indicating that a small fraction of RIP1, but not total RIP1, is targeted by IAPs.”
- Essential versus accessory aspects of cell death: recommendations of the NCCD 2015 (2014, background): “In comparatively more physiologic conditions, however, the fate of cells exposed to death receptor ligands may be determined by the activation kinetics of mitogen-activated protein kinase kinase kinase 7 (MAP3K7, best known as TGFb-activated kinase 1, TAK1),(192,193,207) which normally initiates a c”
- Molecular mechanisms of necroptosis: an ordered cellular explosion (2010, background): “cIAPs catalyse the addition of Lys63-linked polyubiquitin moieties to Lys377 of RIP1 (Ref”
- Ubiquitylation in innate and adaptive immunity (2009, background): “Recent studies suggest that cIAP1 and cIAP2 can catalyse the polyubiquitylation of RIP1 and are required for IKK activation by TNF-&alpha”
- Life and death by death receptors (2009, background): “Consistently, it has recently been shown that cIAP-1and cIAP-2 directly ubiquitinate RIP1 and induce constitutive RIP1 polyubiquitination in cancer cells, therefore sustaining cancer cell proliferation (144).”