Covalent cross-linking of kinases with their corresponding peptide substrates

Alexander V. Statsuk, Kevan M. Shokat*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

Abstract

Protein phosphorylation represents the most dominant and evolutionary conserved posttranslational modification for information transfer in cells and organisms. The human genome encodes >500 protein kinases, and thousands of phosphorylation sites are present in mammalian proteome. To develop a global view of phosphorylation network, there is a need to map the connectivity between kinases and phosphoproteome. We developed a chemical kinase-substrate cross-linker 1 that converts transient kinase-substrate interactions into a covalently linked kinase-substrate complex in vitro and in the presence of cell lysates. The method can be applied to identify unknown upstream kinases responsible for phosphorylation events in cell lysates.

Original languageEnglish (US)
Title of host publicationKinase Inhibitors
Subtitle of host publicationMethods and Protocols
EditorsBernhard Kuster
Pages179-190
Number of pages12
DOIs
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
Volume795
ISSN (Print)1064-3745

Keywords

  • Covalent cross-link
  • Kinase
  • Kinase inhibitor
  • Substrate
  • Thiophene-2,3-dialdehyde

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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