title: Caspase substrates: easily caught in deep waters?
abstract: Caspases are key players in various cellular processes, such as apoptosis, proliferation and differentiation, and in pathological conditions including cancer and inflammation. Although caspases preferentially cleave C-terminal of aspartic acid residues, their action is restricted generally to one or a few sites per protein substrate. Caspase-specific substrate recognition appears to be determined by the substrate sequences adjacent to the scissile bond. Knowledge of these substrates and the generated fragments is crucial for a thorough understanding of the functional implications of caspase-mediated proteolysis. In addition, insight into the cleavage specificity might assist in designing inhibitors that target disease-related caspase activities. Here, we critically review recently published procedures used to generate a proteome-wide view of caspase substrates.
authors.affiliation: Department for Molecular Biomedical Research, VIB, B-9052 Ghent, Belgium.
authors.forename: Dieter
authors.initials: D
authors.lastname: Demon
authors.forename: Petra
authors.initials: P
authors.lastname: Van Damme
authors.forename: Tom
authors.initials: T
authors.lastname: Vanden Berghe
authors.forename: Joël
authors.initials: J
authors.lastname: Vandekerckhove
authors.forename: Wim
authors.initials: W
authors.lastname: Declercq
authors.forename: Kris
authors.initials: K
authors.lastname: Gevaert
authors.forename: Peter
authors.initials: P
authors.lastname: Vandenabeele
mesh_terms: D020169:Caspases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013379:Substrate Specificity
chemical_list: D011506:Proteins; D020169:Caspases