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Kinase inhibition profiles as a tool to identify kinases for specific phosphorylation sites

Nature communications, 2020-04, Vol.11 (1), p.1684-1684, Article 1684 [Peer Reviewed Journal]

The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2020 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-020-15428-0 ;PMID: 32245944

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Title:
Kinase inhibition profiles as a tool to identify kinases for specific phosphorylation sites
Author: Watson, Nikolaus A ; Cartwright, Tyrell N ; Lawless, Conor ; Cámara-Donoso, Marcos ; Sen, Onur ; Sako, Kosuke ; Hirota, Toru ; Kimura, Hiroshi ; Higgins, Jonathan M G
Subjects: Chromosomal Proteins, Non-Histone - metabolism ; Cyclin B ; DNA-Binding Proteins - metabolism ; Enzyme Assays ; Epidermal growth factor receptors ; Genetic screening ; Genetic Testing - methods ; HeLa Cells ; High-Throughput Screening Assays - methods ; Humans ; INCENP protein ; Kinases ; Mitosis ; Phosphorylation ; Phosphorylation - drug effects ; Protein kinase A ; Protein Kinase Inhibitors - pharmacology ; Protein Kinases - metabolism ; Recombinant Proteins - metabolism ; Substrates ; Transcription Factors - metabolism
Is Part Of: Nature communications, 2020-04, Vol.11 (1), p.1684-1684, Article 1684
Description: There are thousands of known cellular phosphorylation sites, but the paucity of ways to identify kinases for particular phosphorylation events remains a major roadblock for understanding kinase signaling. To address this, we here develop a generally applicable method that exploits the large number of kinase inhibitors that have been profiled on near-kinome-wide panels of protein kinases. The inhibition profile for each kinase provides a fingerprint that allows identification of unknown kinases acting on target phosphosites in cell extracts. We validate the method on diverse known kinase-phosphosite pairs, including histone kinases, EGFR autophosphorylation, and Integrin β1 phosphorylation by Src-family kinases. We also use our approach to identify the previously unknown kinases responsible for phosphorylation of INCENP at a site within a commonly phosphorylated motif in mitosis (a non-canonical target of Cyclin B-Cdk1), and of BCL9L at S915 (PKA). We show that the method has clear advantages over in silico and genetic screening.
Publisher: England: Nature Publishing Group
Language: English
Identifier: ISSN: 2041-1723
EISSN: 2041-1723
DOI: 10.1038/s41467-020-15428-0
PMID: 32245944
Source: MEDLINE
PubMed Central
ProQuest Central
DOAJ Directory of Open Access Journals

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Kinase inhibition profiles as a tool to identify kinases for specific phosphorylation sites

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