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000141293 041__ $$aEnglish
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000141293 1001_ $$0P:(DE-HGF)0$$aCrawford, E. D.$$b0
000141293 245__ $$aConservation of caspase substrates across metazoans suggests hierarchical importance of signaling pathways over specific targets and cleavage site motifs in apoptosis.
000141293 260__ $$aLondon$$bMacmillan$$c2012
000141293 264_1 $$2Crossref$$3online$$bSpringer Science and Business Media LLC$$c2012-08-24
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000141293 520__ $$aCaspases, cysteine proteases with aspartate specificity, are key players in programmed cell death across the metazoan lineage. Hundreds of apoptotic caspase substrates have been identified in human cells. Some have been extensively characterized, revealing key functional nodes for apoptosis signaling and important drug targets in cancer. But the functional significance of most cuts remains mysterious. We set out to better understand the importance of caspase cleavage specificity in apoptosis by asking which cleavage events are conserved across metazoan model species. Using N-terminal labeling followed by mass spectrometry, we identified 257 caspase cleavage sites in mouse, 130 in Drosophila, and 50 in Caenorhabditis elegans. The large majority of the caspase cut sites identified in mouse proteins were found conserved in human orthologs. However, while many of the same proteins targeted in the more distantly related species were cleaved in human orthologs, the exact sites were often different. Furthermore, similar functional pathways are targeted by caspases in all four species. Our data suggest a model for the evolution of apoptotic caspase specificity that highlights the hierarchical importance of functional pathways over specific proteins, and proteins over their specific cleavage site motifs.
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000141293 650_7 $$0EC 3.4.22.-$$2NLM Chemicals$$aCaspases
000141293 650_2 $$2MeSH$$aAnimals
000141293 650_2 $$2MeSH$$aApoptosis
000141293 650_2 $$2MeSH$$aCaenorhabditis elegans: enzymology
000141293 650_2 $$2MeSH$$aCaspases: metabolism
000141293 650_2 $$2MeSH$$aCell Line
000141293 650_2 $$2MeSH$$aDrosophila: enzymology
000141293 650_2 $$2MeSH$$aHumans
000141293 650_2 $$2MeSH$$aMass Spectrometry
000141293 650_2 $$2MeSH$$aMice
000141293 650_2 $$2MeSH$$aSignal Transduction
000141293 650_2 $$2MeSH$$aSubstrate Specificity
000141293 7001_ $$aSeaman, J. E.$$b1
000141293 7001_ $$aBarber, A. E.$$b2
000141293 7001_ $$0P:(DE-2719)2810353$$aDavid, Della$$b3$$udzne
000141293 7001_ $$aBabbitt, P. C.$$b4
000141293 7001_ $$aBurlingame, A. L.$$b5
000141293 7001_ $$0P:(DE-HGF)0$$aWells, J. A.$$b6$$eCorresponding author
000141293 77318 $$2Crossref$$3journal-article$$a10.1038/cdd.2012.99$$b : Springer Science and Business Media LLC, 2012-08-24$$n12$$p2040-2048$$tCell Death & Differentiation$$v19$$x1350-9047$$y2012
000141293 773__ $$0PERI:(DE-600)1496681-5$$a10.1038/cdd.2012.99$$gVol. 19, no. 12, p. 2040 - 2048$$n12$$p2040-2048$$q19:12<2040 - 2048$$tCell death and differentiation$$v19$$x1350-9047$$y2012
000141293 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3504717
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