A Microarray Strategy for Mapping the Substrate Specificity of Protein Tyrosine Phosphatase

摘要

Reversible phosphorylation of tyrosine residues in proteins is involved in regulating numerous cellular events, such as cell growth, cell differentiation, cell-cycle regulation, cellular signal transduction, cell adhesion, and the immune response. Phosphorylation is controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Although PTKs have been studied extensively, knowledge about PTP substrate specificities is still limited. The corresponding data could be used to create artificial substrates for kinetic studies, to design inhibitors leading to drug candidates and tools to investigate PTP pathways in cells, and might even give hints for the identification of natural substrates. Several peptide-based approaches have been reported for mapping PTP substrate specificity.