Bio-orthogonal affinity purification of direct kinase substrates

J Am Chem Soc. 2005 Apr 20;127(15):5288-9. doi: 10.1021/ja050727t.

Abstract

Protein phosphorylation is a major mechanism of post-translational protein modification used to control cellular signaling. A challenge in phosphoproteomics is to identify the direct substrates of each protein kinase. Herein, we describe a chemical strategy for delivery of a bio-orthogonal affinity tag to the substrates of an individual protein kinase. The kinase of interest is engineered to transfer a phosphorothioate moiety to phosphoacceptor hydroxyl groups on direct substrates. In a second nonenzymatic step, the introduced phosphorothioate is alkylated with p-nitrobenzylmesylate (PNBM). Antibodies directed against the alkylated phosphorothioate epitope recognize these labeled substrates, but not alkylation products of other cellular nucleophiles. This strategy is demonstrated with Cdk1/cyclinB substrates using ELISA, western blotting, and immunoprecipitation in the context of whole cell lysates.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives*
  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Affinity Labels / chemistry*
  • Affinity Labels / metabolism
  • CDC2 Protein Kinase / metabolism*
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / isolation & purification
  • Cell Cycle Proteins / metabolism
  • HeLa Cells
  • Histones / chemistry*
  • Histones / isolation & purification
  • Histones / metabolism
  • Humans
  • Immunoconjugates / chemistry*
  • Immunoconjugates / metabolism
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / metabolism
  • Immunoglobulins / chemistry
  • Immunoglobulins / metabolism
  • Mesylates / chemistry
  • Protein-Tyrosine Kinases / chemistry*
  • Protein-Tyrosine Kinases / isolation & purification
  • Protein-Tyrosine Kinases / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / isolation & purification
  • Saccharomyces cerevisiae Proteins / metabolism
  • Substrate Specificity

Substances

  • Affinity Labels
  • Cell Cycle Proteins
  • Histones
  • IgY
  • Immunoconjugates
  • Immunoglobulin G
  • Immunoglobulins
  • Mesylates
  • Saccharomyces cerevisiae Proteins
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • SWE1 protein, S cerevisiae
  • Protein-Tyrosine Kinases
  • CDC2 Protein Kinase