ArticleLife science alliance2022
Systematic identification of ALK substrates by integrated phosphoproteome and interactome analysis.
Article in Life science alliance, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Predicting hypertension through big five personality traits: a four-year longitudinal study in Japan.BMC psychology · 2025Article
- Establishment of enterotype-specific antibodies for various diagnostic systems.Scientific reports · 2025Article
- Identification of APBB1 as a substrate for anaplastic lymphoma kinase.Journal of biochemistry · 2024Article
- Phosphoproteomic Analysis Identified Mutual Phosphorylation of FAK and Src as a Mechanism of Osimertinib Resistance inJTO clinical and research reports · 2024Article
- QcrC is a potential target for antibody therapy and vaccination to controlFrontiers in microbiology · 2024Article
- Systematic Identification of Kinase-Substrate Relationship by Integrated Phosphoproteome and Interactome Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Validity of the cell-extracted proteome as a substrate pool for exploring phosphorylation motifs of kinases.Genes to cells : devoted to molecular & cellular mechanisms · 2023Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sensitivity of phosphorylation site identification by mass spectrometry has improved markedly. However, the lack of kinase-substrate relationship (KSR) data hinders the improvement of the range and accuracy of kinase activity prediction. In this study, we aimed to develop a method for acquiring systematic KSR data on anaplastic lymphoma kinase (ALK) using mass spectrometry and to apply this method to the prediction of kinase activity. Thirty-seven ALK substrate candidates, including 34 phosphorylation sites not annotated in the PhosphoSitePlus database, were identified by integrated analysis of the phosphoproteome and crosslinking interactome of HEK 293 cells with doxycycline-induced ALK overexpression. Furthermore, KSRs of ALK were validated by an in vitro kinase assay. Finally, using phosphoproteomic data from ALK mutant cell lines and patient-derived cells treated with ALK inhibitors, we found that the prediction of ALK activity was improved when the KSRs identified in this study were used instead of the public KSR dataset. Our approach is applicable to other kinases, and future identification of KSRs will facilitate more accurate estimations of kinase activity and elucidation of phosphorylation signals.
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