ArticleCell reports2026
Kinase condensates enrich ATP and trigger autophosphorylation.
Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Review
- Spatial biology of crowded tumor cells: A new map for designing drug combinations.Current opinion in structural biology · 2026Review
- AI-discovered protein fragments as generalizable regulators of biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Kinase-mediated signal transduction regulates most cellular processes, and concentration-dependent autophosphorylation is a common mechanism to promote kinase signaling. Many kinases undergo phase separation to form condensates. Despite the central role of autophosphorylation in regulating kinase activity, how condensates impact kinase autophosphorylation has not been systematically studied. Using biochemical reconstitution and cellular studies, we find that phase separation can concentrate kinases to effectively trigger the trans-autophosphorylation of the tyrosine kinases FAK and Abl, as well as the serine/threonine kinase Mst2. Moreover, kinase condensates can create a chemical environment that enriches ATP, and positively charged intrinsically disordered regions are one feature that enrich ATP into condensates. Thus, kinase phase separation is a general mechanism to activate kinase signaling pathways by locally concentrating both kinases and ATP to trigger autophosphorylation.
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