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http://purl.uniprot.org/citations/17371877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17371877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17371877http://www.w3.org/2000/01/rdf-schema#comment"Genetic studies have established that the cysteine protease CED-3 plays a central role in coordinating programmed cell death in Caenorhabditis elegans. However, it remains unclear how CED-3 activation results in cell death because few substrates for this protease have been described. We have used a global proteomics approach to seek substrates for CED-3 and have identified 22 worm proteins that undergo CED-3-dependent proteolysis. Proteins that were found to be substrates for CED-3 included the cytoskeleton proteins actin, myosin light chain, and tubulin, as well as proteins involved in ATP synthesis, cellular metabolism, and chaperone function. We estimate that approximately 3% of the C. elegans proteome is susceptible to CED-3-dependent proteolysis. Notably, the endoplasmic reticulum chaperone calreticulin, which has been implicated in the recognition of apoptotic cells by phagocytes, was cleaved by CED-3 and was also cleaved by human caspases during apoptosis. Inhibitors of caspase activity blocked the appearance of calreticulin on the surface of apoptotic cells, suggesting a mechanism for the surface display of calreticulin during apoptosis. Further analysis of these substrates is likely to yield important insights into the mechanism of killing by CED-3 and its human caspase counterparts."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m611051200"xsd:string
http://purl.uniprot.org/citations/17371877http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m611051200"xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Brumatti G."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Brumatti G."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Derry W.B."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Derry W.B."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Hengartner M.O."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Hengartner M.O."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Martin S.J."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Martin S.J."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Taylor R.C."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/author"Taylor R.C."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/pages"15011-15021"xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/pages"15011-15021"xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/title"Establishing a blueprint for CED-3-dependent killing through identification of multiple substrates for this protease."xsd:string
http://purl.uniprot.org/citations/17371877http://purl.uniprot.org/core/title"Establishing a blueprint for CED-3-dependent killing through identification of multiple substrates for this protease."xsd:string