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Methods Mol Biol. 2012;795:179-90. doi: 10.1007/978-1-61779-337-0_12.

Covalent cross-linking of kinases with their corresponding peptide substrates.

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Department of Chemistry, Northwestern University, Evanston, IL, USA.


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.

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