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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAbGSDt5ljipSrbPM4sKgyrRDLlqWiPAx5SPulnIdVlKk#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAbGSDt5ljipSrbPM4sKgyrRDLlqWiPAx5SPulnIdVlKk#_5 http://www.w3.org/ns/prov#value Figure 3 | Neuronal anti-apoptotic brakes upstream of mitochondria. Black lines represent apoptotic pathways,blue lines represent survival pathways and red lines indicate inhibition or activation (arrows). TNF? (tumour necrosis factor-?)- and FASL (apoptosis antigen-1 (FAS) ligand) mediated death can be suppressed by sequestration by decoy receptors; FASL can bind to DCR3 (decoy receptor 3) or FDR (FAS decoy receptor), or to MET3, a HGF (hepatocyte growth factor) receptor,resulting in no downstream signalling. TNFR2 (tumour necrosis factor receptor 2) can be cleaved by metalloproteases into a soluble decoy receptor for TNF?, and TNF? signalling through the TNFR1 RIP TRAF2 (TNF receptor 1 receptor interacting protein TNF receptor associated factor 2) complex is inhibited by FLIP (FLICE-inhibitory protein), IAPs (inhibitor of apoptosis proteins) and HSP90 (heat shock protein 90). FLIP also prevents recruitment of procaspase 8 to FADD (FAS-associated death domain), inhibiting apoptosis by the TNFa FADD and Fas FADD pathways. Activation of procaspase 8 to caspase 8 is inhibited by BCL2 (B-cell leukaemia/lymphoma-2) and APC (activated protein C), preventing cleavage of BID (BH3 interacting domain death agonist) to tBID (truncated BID). tBID translocation to the mitochondrion is prevented by stabilization of the cytoskeletal networks by HSP27 (heat shock protein 27). FAS-associated phosphatase-1 (FAP1) prevents binding of FADD and DAXX (death-associated protein) to FAS, and HSP27 inhibits DAXX-mediated activation of ASK1 (apoptosis signal regulated kinase-1) and the JNK (c-Jun-N-teminal kinase)-death pathway. JNK activity is inhibited by HSP70 and its co-chaperone HSP40, and by the IAPs NIAP (neuronal IAP) and XIAP (X-chromosome linked IAP), with XIAP in a complex with its binding partners TAK1 (TGF?-activated kinase) and TAB1 (TAK1-binding protein). ER (endoplasmic reticulum)- mediated apoptosis is inhibited by ORP150 (oxygen regulated protein 150), which prevents activation of calcium-dependent proteases, and by BCL2 and BAR (bifunctional apoptosis regulator)-mediated suppression of BAP31 (B-cell receptorassociated protein 31). IAP proteins negatively regulate pro-death p75NTR (p75 neurotrophin receptor) signalling through NRAGE (neurotrophin receptor interacting MAGE homologue), preventing signalling through the JNK-death pathway. XIAP mediates survival (blue lines) by binding to the cytoplasmic domain of BMP (bone morphogenic protein) receptors, which recruit TAB1 and TAK1 to activate the NF-?B (nuclear factor-?B) survival pathway. IAPs, HSP27 and HSP90 bind to AKT/PKB (protein kinase B) to promote the AKT survival pathway (blue lines). 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