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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.

SUBMITTER: Dedigama-Arachchige PM

PROVIDER: S-EPMC5481203 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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K-CLASP: A Tool to Identify Phosphosite Specific Kinases and Interacting Proteins.

Dedigama-Arachchige Pavithra M PM Pflum Mary Kay H MK

ACS chemical biology 20161017 12

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 ...[more]

PMID: 27726338

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