Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases.

ABSTRACT: Protein phosphorylation is dynamically regulated by the opposing activities of phosphowriter enzymes (kinases) and phosphoeraser enzymes (phosphatases and phospholyases). While significant progress has been made toward defining the sequences preferences of kinases, the selectivity of phosphoerasers has not been explored at scale. Here, we develop an experimental platform based on tandem mass spectrometry analysis of phosphoproteome-derived peptide libraries (PhosPropels) to map phosphoeraser activity across thousands of biologically relevant phosphosites. We extract positional residue preferences to rapidly define sequence motifs recognized by eight phosphoerasers spanning diverse species of origin, protein folds, and enzymatic mechanisms. Taking advantage of the throughput of our approach

SUBMITTER: Radziwon K 

PROVIDER: S-EPMC12363953 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature