High-throughput screening of substrate specificity for protein tyrosine phosphatases (PTPs) on phosphopeptide microarrays

Liqian Gao, Su Seong Lee, Jun Chen, Hongyan Sun, Yuliang Zhao, Zhifang Chai, Yi Hu

Research output: Chapter in Book/Report/Conference proceedingChapter

15 Scopus citations


Phosphatases are a family of enzymes responsible for the dephosphorylation of biomolecules. Phosphatases play essential roles in cell cycle regulation, signal transduction, and cellular communication. In recent years, one type of phosphatases, protein tyrosine phosphatases (PTPs), emerges as important therapeutic targets for complex and devastating diseases. Nevertheless, the physiological roles, substrate specificity, and downstream targets for PTPs remain largely unknown. To demonstrate how microarrays can be applied to characterizing PTPs, we describe here a phosphopeptide microarray strategy for activity-based high-throughput screening of PTPs substrate specificity. This is followed by a kinetic microarray assay and microplate assay to determine the rate constants of dephosphorylation by PTPs. This microarray strategy has been successfully applied to identifying several potent and selective substrates against different PTPs. These substrates could be used to design potent and selective PTPs inhibitors in the future.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press
Number of pages16
StatePublished - May 1 2016

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • High-throughput screening
  • Phosphopeptide microarrays
  • Protein tyrosine phosphatases
  • Substrate specificity

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


Dive into the research topics of 'High-throughput screening of substrate specificity for protein tyrosine phosphatases (PTPs) on phosphopeptide microarrays'. Together they form a unique fingerprint.

Cite this