Proteome-wide identification of family member-specific natural substrate repertoire of caspases.

ABSTRACT: Caspases are proteolytic enzymes that are essential for apoptosis. Understanding the many discrete and interacting signaling pathways mediated by caspases requires the identification of the natural substrate repertoire for each caspase of interest. Using an amplification-based protein selection technique called mRNA display, we developed a high-throughput screen platform for caspase family member specific substrates on a proteome-wide scale. A large number of both known and previously uncharacterized caspase-3 substrates were identified from the human proteome. The proteolytic features of these selected substrates, including their cleavage sites and specificities, were characterized. Substrates that were cleaved only by caspase-8 or granzyme B but not by caspase-3, were readily selected. T

SUBMITTER: Ju W 

PROVIDER: S-EPMC1958819 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature