ArticleChembiochem : a European journal of chemical biology2017
K-BILDS: A Kinase Substrate Discovery Tool.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Proteomic approaches for protein kinase substrate identification in Apicomplexa.Molecular and biochemical parasitology · 2024Review
- Deep PIM kinase substrate profiling reveals new rational cotherapeutic strategies for acute myeloid leukemia.Blood advances · 2024Article
- Kinase-catalyzed biotinylation for discovery and validation of substrates to multispecificity kinases NME1 and NME2.The Journal of biological chemistry · 2024Article
- DeKinomics pulse-chases kinase functions in living cells.Nature chemical biology · 2024Article
- The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Kinase-Catalyzed Biotinylation to Identify Phosphatase Substrates (K-BIPS).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Phosphoproteomic Approaches for Identifying Phosphatase and Kinase Substrates.Molecules (Basel, Switzerland) · 2023Review
- Kinase-Catalyzed Crosslinking and Immunoprecipitation (K-CLIP) to Explore Kinase-Substrate Pairs.Current protocols · 2022Article
- Kinase-Catalyzed Biotinylation to Map Cell Signaling Pathways: Application to Epidermal Growth Factor Signaling.Journal of proteome research · 2021Article
- Accurate prediction of kinase-substrate networks using knowledge graphs.PLoS computational biology · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kinases catalyze protein phosphorylation to regulate cell signaling events. However, identifying kinase substrates is challenging due to the often low abundance and dynamic nature of protein phosphorylation. Development of novel techniques to identify kinase substrates is necessary. Here, we report kinase-catalyzed biotinylation with inactivated lysates for discovery of substrates (K-BILDS) as a tool to identify direct substrates of a kinase. As a proof of concept, K-BILDS was applied to cAMP-dependent protein kinase A (PKA) with HeLa cell lysates. Subsequent enrichment and MS/MS analysis identified 279 candidate PKA substrates, including 56 previously known PKA substrates. Of the candidate substrates, nuclear autoantigenic sperm protein (NASP), BCL2-associated athanogene 3 (BAG3), and 14-3-3 protein Tau (YWHAQ) were validated as novel PKA substrates. K-BILDS provides a valuable tool to identify direct substrates of any protein kinase.
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