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@ARTICLE{Crawford:141293,
      author       = {Crawford, E. D. and Seaman, J. E. and Barber, A. E. and
                      David, Della and Babbitt, P. C. and Burlingame, A. L. and
                      Wells, J. A.},
      title        = {{C}onservation of caspase substrates across metazoans
                      suggests hierarchical importance of signaling pathways over
                      specific targets and cleavage site motifs in apoptosis.},
      journal      = {Cell death and differentiation},
      volume       = {19},
      number       = {12},
      issn         = {1350-9047},
      address      = {London},
      publisher    = {Macmillan},
      reportid     = {DZNE-2020-07615},
      pages        = {2040-2048},
      year         = {2012},
      abstract     = {Caspases, 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.},
      keywords     = {Animals / Apoptosis / Caenorhabditis elegans: enzymology /
                      Caspases: metabolism / Cell Line / Drosophila: enzymology /
                      Humans / Mass Spectrometry / Mice / Signal Transduction /
                      Substrate Specificity / Caspases (NLM Chemicals)},
      cin          = {AG David},
      ddc          = {610},
      cid          = {I:(DE-2719)1210004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22918439},
      pmc          = {pmc:PMC3504717},
      doi          = {10.1038/cdd.2012.99},
      url          = {https://pub.dzne.de/record/141293},
}