Using Peptide Arrays to Profile Phosphatase Activity in Cell Lysates

Lindsey C. Szymczak, Daniel J. Sykora, Milan Mrksich*

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Phosphorylation is an important post-translational modification on proteins involved in many cellular processes; however, understanding of the regulation and mechanisms of global phosphorylation remains limited. Herein, we utilize self-assembled monolayers on gold for matrix-assisted laser desorption/ionization mass spectrometry (SAMDI-MS) with three phosphorylated peptide arrays to profile global phosphatase activity in cell lysates derived from five mammalian cell lines. Our results reveal significant differences in the activities of protein phosphatases on phospho- serine, threonine, and tyrosine substrates and suggest that phosphatases play a much larger role in the regulation of global phosphorylation on proteins than previously understood.

Original languageEnglish (US)
Pages (from-to)165-170
Number of pages6
JournalChemistry - A European Journal
Volume26
Issue number1
DOIs
StatePublished - Jan 2 2020

Keywords

  • SAMDI-MS
  • cell lysates
  • high-throughput screening
  • phosphatases
  • phosphorylation

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

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