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http://purl.uniprot.org/citations/20956541http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20956541http://www.w3.org/2000/01/rdf-schema#comment"Acid sphingomyelinase (A-SMase) is an important enzyme in sphingolipid metabolism and plays key roles in apoptosis, immunity, development, and cancer. In addition, it mediates cytotoxicity of cisplatin and some other chemotherapeutic drugs. The mechanism of A-SMase activation is still undefined. We now demonstrate that, upon CD95 stimulation, A-SMase is activated through translocation from intracellular compartments to the plasma membrane in an exocytic pathway requiring the t-SNARE protein syntaxin 4. Indeed, down-regulation of syntaxin 4 inhibits A-SMase translocation and activation induced by CD95 stimulation. This leads to inhibition of the CD95-triggered signaling events, including caspase 3 and 9 activation and apoptosis, activation of the survival pathway involving the protein kinase Akt, and important changes in cell cycle and proliferation. The molecular interaction between A-SMase and syntaxin 4 was not known and clarifies the mechanism of A-SMase activation. The novel actions of syntaxin 4 in sphingolipid metabolism and exocytosis we describe here define signaling mechanisms of broad relevance in cell pathophysiology."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.139287"xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Rosa P."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Bassi M.T."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Gulbins E."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Perrotta C."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Simbari F."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Clementi E."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Morlacchi S."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Bizzozero L."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Assi E."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/author"Cazzato D."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/pages"40240-40251"xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/title"Syntaxin 4 is required for acid sphingomyelinase activity and apoptotic function."xsd:string
http://purl.uniprot.org/citations/20956541http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20956541http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20956541
http://purl.uniprot.org/citations/20956541http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20956541
http://purl.uniprot.org/uniprot/P17405#attribution-9851849ADB61F075738F88A84E3B7474http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20956541
http://purl.uniprot.org/uniprot/P11279#attribution-9851849ADB61F075738F88A84E3B7474http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20956541
http://purl.uniprot.org/uniprot/Q12846#attribution-45A3808D6322E19D253DBE0110D7271Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20956541
http://purl.uniprot.org/uniprot/Q12846#attribution-9851849ADB61F075738F88A84E3B7474http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20956541