| Literature DB >> 27726338 |
Pavithra M Dedigama-Arachchige1, Mary Kay H Pflum1.
Abstract
Few methods are available to discover the cellular kinase that phosphorylates a specific amino acid, or phosphosite, on a protein. In addition, identifying the associated proteins bound near a phosphosite during phosphorylation would provide insights into cell biology and signaling. Here, we report K-CLASP (Kinase Catalyzed CrossLinking And Streptavidin Purification) as a method for both phosphosite-specific kinase identification and the discovery of kinase interacting proteins. K-CLASP offers a powerful tool to discover unanticipated protein-protein interactions in phosphorylation-mediated biological events.Entities:
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Year: 2016 PMID: 27726338 PMCID: PMC5481203 DOI: 10.1021/acschembio.6b00289
Source DB: PubMed Journal: ACS Chem Biol ISSN: 1554-8929 Impact factor: 5.100