PMC:3585731 / 41618-42881 JSONTXT

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This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T21058","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T21057","span":{"begin":813,"end":817},"obj":"Protein"},{"id":"T21056","span":{"begin":719,"end":726},"obj":"Protein"},{"id":"T21055","span":{"begin":651,"end":658},"obj":"Protein"},{"id":"T21054","span":{"begin":376,"end":380},"obj":"Protein"},{"id":"T21053","span":{"begin":249,"end":253},"obj":"Protein"},{"id":"T21052","span":{"begin":105,"end":109},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T22936","span":{"begin":813,"end":817},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T22935","span":{"begin":376,"end":380},"obj":"http://www.uniprot.org/uniprot/P01375"},{"id":"T22920","span":{"begin":839,"end":843},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T22919","span":{"begin":249,"end":253},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T22918","span":{"begin":105,"end":109},"obj":"http://www.uniprot.org/uniprot/Q13546"},{"id":"T22858","span":{"begin":1131,"end":1134},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22857","span":{"begin":1008,"end":1011},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22856","span":{"begin":909,"end":912},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22855","span":{"begin":723,"end":726},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22854","span":{"begin":655,"end":658},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22824","span":{"begin":1131,"end":1134},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22823","span":{"begin":1008,"end":1011},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22822","span":{"begin":909,"end":912},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22821","span":{"begin":723,"end":726},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22820","span":{"begin":655,"end":658},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22819","span":{"begin":592,"end":595},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22818","span":{"begin":459,"end":462},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22817","span":{"begin":186,"end":189},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22816","span":{"begin":37,"end":40},"obj":"http://www.uniprot.org/uniprot/P31749"},{"id":"T22888","span":{"begin":655,"end":658},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22887","span":{"begin":592,"end":595},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22886","span":{"begin":459,"end":462},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22885","span":{"begin":186,"end":189},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22884","span":{"begin":37,"end":40},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22853","span":{"begin":592,"end":595},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22852","span":{"begin":459,"end":462},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22851","span":{"begin":186,"end":189},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22850","span":{"begin":37,"end":40},"obj":"http://www.uniprot.org/uniprot/P31751"},{"id":"T22892","span":{"begin":1131,"end":1134},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22891","span":{"begin":1008,"end":1011},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22890","span":{"begin":909,"end":912},"obj":"http://www.uniprot.org/uniprot/Q9Y243"},{"id":"T22889","span":{"begin":723,"end":726},"obj":"http://www.uniprot.org/uniprot/Q9Y243"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"GO-BP","denotations":[{"id":"T21200","span":{"begin":576,"end":588},"obj":"http://purl.obolibrary.org/obo/GO_0051179"},{"id":"T21199","span":{"begin":567,"end":588},"obj":"http://purl.obolibrary.org/obo/GO_0051668"},{"id":"T21198","span":{"begin":560,"end":588},"obj":"http://purl.obolibrary.org/obo/GO_0072659"},{"id":"T21197","span":{"begin":560,"end":588},"obj":"http://purl.obolibrary.org/obo/GO_0044856"},{"id":"T21196","span":{"begin":531,"end":537},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T21180","span":{"begin":1257,"end":1262},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T21179","span":{"begin":409,"end":414},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T21168","span":{"begin":1252,"end":1262},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T21167","span":{"begin":404,"end":414},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T21163","span":{"begin":818,"end":827},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T21162","span":{"begin":381,"end":390},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T21157","span":{"begin":805,"end":808},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T21156","span":{"begin":350,"end":353},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T21138","span":{"begin":1188,"end":1199},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T21137","span":{"begin":766,"end":777},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T21136","span":{"begin":313,"end":324},"obj":"http://purl.obolibrary.org/obo/GO_0097528"},{"id":"T21131","span":{"begin":753,"end":777},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T21114","span":{"begin":1188,"end":1199},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T21113","span":{"begin":766,"end":777},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T21112","span":{"begin":313,"end":324},"obj":"http://purl.obolibrary.org/obo/GO_0070266"},{"id":"T21106","span":{"begin":979,"end":994},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T21105","span":{"begin":890,"end":905},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T21104","span":{"begin":440,"end":455},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T21103","span":{"begin":190,"end":205},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T21095","span":{"begin":956,"end":965},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T21094","span":{"begin":275,"end":284},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T21093","span":{"begin":79,"end":88},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"GO-MF","denotations":[{"id":"T21268","span":{"begin":805,"end":808},"obj":"http://purl.obolibrary.org/obo/GO_0004705"},{"id":"T21267","span":{"begin":350,"end":353},"obj":"http://purl.obolibrary.org/obo/GO_0004705"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"GO-CC","denotations":[{"id":"T21293","span":{"begin":1166,"end":1172},"obj":"http://purl.obolibrary.org/obo/GO_0031931"},{"id":"T21291","span":{"begin":633,"end":641},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T21290","span":{"begin":567,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T21288","span":{"begin":560,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0005886"},{"id":"T21279","span":{"begin":1096,"end":1101},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T21278","span":{"begin":333,"end":338},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"sentences","denotations":[{"id":"T20940","span":{"begin":967,"end":1263},"obj":"Sentence"},{"id":"T20939","span":{"begin":829,"end":966},"obj":"Sentence"},{"id":"T20938","span":{"begin":687,"end":828},"obj":"Sentence"},{"id":"T20937","span":{"begin":494,"end":686},"obj":"Sentence"},{"id":"T20936","span":{"begin":416,"end":493},"obj":"Sentence"},{"id":"T20935","span":{"begin":217,"end":415},"obj":"Sentence"},{"id":"T20934","span":{"begin":0,"end":216},"obj":"Sentence"},{"id":"T258","span":{"begin":0,"end":216},"obj":"Sentence"},{"id":"T259","span":{"begin":217,"end":415},"obj":"Sentence"},{"id":"T260","span":{"begin":416,"end":493},"obj":"Sentence"},{"id":"T261","span":{"begin":494,"end":596},"obj":"Sentence"},{"id":"T262","span":{"begin":597,"end":686},"obj":"Sentence"},{"id":"T263","span":{"begin":687,"end":828},"obj":"Sentence"},{"id":"T264","span":{"begin":829,"end":966},"obj":"Sentence"},{"id":"T265","span":{"begin":967,"end":1263},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"simple1","denotations":[{"id":"T21310","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T21309","span":{"begin":813,"end":817},"obj":"Protein"},{"id":"T21308","span":{"begin":719,"end":726},"obj":"Protein"},{"id":"T21307","span":{"begin":651,"end":658},"obj":"Protein"},{"id":"T21306","span":{"begin":376,"end":380},"obj":"Protein"},{"id":"T21305","span":{"begin":249,"end":253},"obj":"Protein"},{"id":"T21304","span":{"begin":105,"end":109},"obj":"Protein"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T22798","span":{"begin":705,"end":715},"obj":"Gene_expression"},{"id":"T22797","span":{"begin":734,"end":744},"obj":"Positive_regulation"},{"id":"T22796","span":{"begin":818,"end":827},"obj":"Gene_expression"},{"id":"T22795","span":{"begin":791,"end":801},"obj":"Positive_regulation"},{"id":"T22794","span":{"begin":597,"end":607},"obj":"Gene_expression"},{"id":"T22793","span":{"begin":633,"end":650},"obj":"Positive_regulation"},{"id":"T22792","span":{"begin":381,"end":390},"obj":"Gene_expression"},{"id":"T22757","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T22756","span":{"begin":813,"end":817},"obj":"Protein"},{"id":"T22755","span":{"begin":719,"end":726},"obj":"Protein"},{"id":"T22754","span":{"begin":651,"end":658},"obj":"Protein"},{"id":"T22753","span":{"begin":376,"end":380},"obj":"Protein"},{"id":"T22752","span":{"begin":249,"end":253},"obj":"Protein"},{"id":"T22751","span":{"begin":105,"end":109},"obj":"Protein"}],"relations":[{"id":"R15381","pred":"themeOf","subj":"T22753","obj":"T22792"},{"id":"R15382","pred":"themeOf","subj":"T22754","obj":"T22794"},{"id":"R15383","pred":"themeOf","subj":"T22754","obj":"T22793"},{"id":"R15384","pred":"themeOf","subj":"T22755","obj":"T22798"},{"id":"R15385","pred":"themeOf","subj":"T22756","obj":"T22796"},{"id":"R15399","pred":"themeOf","subj":"T22796","obj":"T22795"},{"id":"R15400","pred":"themeOf","subj":"T22798","obj":"T22797"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

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This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. 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our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}

{"project":"test3","denotations":[{"id":"T20865","span":{"begin":979,"end":994},"obj":"Phosphorylation"},{"id":"T20864","span":{"begin":890,"end":905},"obj":"Phosphorylation"},{"id":"T20863","span":{"begin":870,"end":878},"obj":"Positive_regulation"},{"id":"T20862","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T20861","span":{"begin":818,"end":827},"obj":"Gene_expression"},{"id":"T20860","span":{"begin":813,"end":817},"obj":"Protein"},{"id":"T20859","span":{"begin":719,"end":726},"obj":"Protein"},{"id":"T20858","span":{"begin":705,"end":715},"obj":"Gene_expression"},{"id":"T20857","span":{"begin":651,"end":658},"obj":"Protein"},{"id":"T20856","span":{"begin":576,"end":588},"obj":"Localization"},{"id":"T20855","span":{"begin":440,"end":455},"obj":"Phosphorylation"},{"id":"T20854","span":{"begin":381,"end":390},"obj":"Gene_expression"},{"id":"T20853","span":{"begin":376,"end":380},"obj":"Protein"},{"id":"T20852","span":{"begin":249,"end":253},"obj":"Protein"},{"id":"T20851","span":{"begin":190,"end":205},"obj":"Phosphorylation"},{"id":"T20850","span":{"begin":174,"end":182},"obj":"Positive_regulation"},{"id":"T20849","span":{"begin":152,"end":161},"obj":"Positive_regulation"},{"id":"T20848","span":{"begin":105,"end":109},"obj":"Protein"},{"id":"T20810","span":{"begin":651,"end":658},"obj":"Protein"},{"id":"T20809","span":{"begin":376,"end":380},"obj":"Protein"},{"id":"T20808","span":{"begin":249,"end":253},"obj":"Protein"},{"id":"T20807","span":{"begin":105,"end":109},"obj":"Protein"},{"id":"T20813","span":{"begin":839,"end":843},"obj":"Protein"},{"id":"T20812","span":{"begin":813,"end":817},"obj":"Protein"},{"id":"T20811","span":{"begin":719,"end":726},"obj":"Protein"}],"relations":[{"id":"R13935","pred":"themeOf","subj":"T20850","obj":"T20849"},{"id":"R13936","pred":"themeOf","subj":"T20851","obj":"T20850"},{"id":"R13937","pred":"themeOf","subj":"T20853","obj":"T20854"},{"id":"R13938","pred":"themeOf","subj":"T20859","obj":"T20858"},{"id":"R13939","pred":"themeOf","subj":"T20860","obj":"T20861"},{"id":"R13940","pred":"themeOf","subj":"T20864","obj":"T20863"}],"text":"Altogether, our results suggest that Akt kinase is specifically engaged in the signaling downstream from RIP1 kinase, which exerts its activity through promoting a selective increase in Akt phosphorylation on Thr308. This provides a link connecting RIP1 kinase to downstream signaling and execution events during necroptosis in L929 cells, including JNK activation, autocrine TNFα synthesis and eventual cell death. According to our model, phosphorylation of Akt requires two distinct signals. The first input, which is induced by growth factors, leads to the plasma membrane localization of Akt. Expression of constitutively active membrane-targeted Myr-Akt overcomes this requirement. At the same time, expression of Myr-Akt is not sufficient for the induction of necroptosis or efficient activation of JNK and TNFα synthesis. A second, RIP1 kinase-dependent input is required for Thr308 phosphorylation of Akt, which in turn is required for necroptotic signaling. Necroptotic phosphorylation of Thr308 of Akt is sufficient to increase its activity towards a number of known substrates in L929 cells and our data reveal that the Akt effector pathway downstream of mTORC1 contributes to necroptosis, thereby identifying a new mediator of this form of cell death."}