Identification of new substrates of the protein-tyrosine phosphatase PTP1B by Bayesian integration of proteome evidence.

ABSTRACT: There is growing evidence that tyrosine phosphatases display an intrinsic enzymatic preference for the sequence context flanking the target phosphotyrosines. On the other hand, substrate selection in vivo is decisively guided by the enzyme-substrate connectivity in the protein interaction network. We describe here a system wide strategy to infer physiological substrates of protein-tyrosine phosphatases. Here we integrate, by a Bayesian model, proteome wide evidence about in vitro substrate preference, as determined by a novel high-density peptide chip technology, and "closeness" in the protein interaction network. This allows to rank candidate substrates of the human PTP1B phosphatase. Ultimately a variety of in vitro and in vivo approaches were used to verify the prediction that the tyros

SUBMITTER: Ferrari E 

PROVIDER: S-EPMC3039405 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature