title: K-CLASP: A Tool to Identify Phosphosite Specific Kinases and Interacting Proteins.
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.
authors.affiliation: Department of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48201, United States.
authors.forename: Pavithra M
authors.initials: PM
authors.lastname: Dedigama-Arachchige
authors.affiliation: Department of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48201, United States.
authors.forename: Mary Kay H
authors.initials: MK
authors.lastname: Pflum
mesh_terms: D001710:Biotin / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D025941:Protein Interaction Mapping / Q000379:methods*; D011494:Protein Kinases / Q000378:metabolism*; D019809:Streptavidin / Q000378:metabolism; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D003432:Cross-Linking Reagents; D010455:Peptides; D001710:Biotin; D019809:Streptavidin; D011494:Protein Kinases