An unbiased proteomic screen reveals caspase cleavage is positively and negatively regulated by substrate phosphorylation.

ABSTRACT: Post-translational modifications of proteins regulate diverse cellular functions, with mounting evidence suggesting that hierarchical cross-talk between distinct modifications may fine-tune cellular responses. For example, in apoptosis, caspases promote cell death via cleavage of key structural and enzymatic proteins that in some instances is inhibited by phosphorylation near the scissile bond. In this study, we systematically investigated how protein phosphorylation affects susceptibility to caspase cleavage using an N-terminomic strategy, namely, a modified terminal amino isotopic labeling of substrates (TAILS) workflow, to identify proteins for which caspase-catalyzed cleavage is modulated by phosphatase treatment. We validated the effects of phosphorylation on three of the identified p

SUBMITTER: Turowec JP 

PROVIDER: S-EPMC4014278 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature