ArticleScience advances2022
Kinetic frustration by limited bond availability controls the LAT protein condensation phase transition on membranes.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- LAT condensation gates PLCγ1 activation via bimodal LAT phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Synthetic FLS2 receptor oligomer boosts plant innate immunity.Science advances · 2026Article
- Article
- A unifying model of LAT condensates in reconstitution experiments.bioRxiv : the preprint server for biology · 2025Article
- Membrane-anchored mobile tethers modulate condensate wetting, localization, and migration.bioRxiv : the preprint server for biology · 2025Article
- Parallel reactions on a single T cell receptor offer a robust kinetic proofreading mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Condensate-membrane interactions shape membranes, tune cytoskeletal assembly, and localize mRNAs.Current opinion in cell biology · 2025Review
- Emerging roles of transcriptional condensates as temporal signal integrators.Nature reviews. Genetics · 2025Review
- Proofreading and single-molecule sensitivity in T cell receptor signaling by condensate nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanical forces amplify TCR mechanotransduction in T cell activation and function.Applied physics reviews · 2024Review
- Two-dimensional molecular condensation in cell signaling and mechanosensing.Acta biochimica et biophysica Sinica · 2023Review
- Self-programmed dynamics of T cell receptor condensation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- DAmFRET measures saturating concentrations and toxicities of protein phase transitions in vivo.Molecular biology of the cell · 2023Article
- A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
LAT is a membrane-linked scaffold protein that undergoes a phase transition to form a two-dimensional protein condensate on the membrane during T cell activation. Governed by tyrosine phosphorylation, LAT recruits various proteins that ultimately enable condensation through a percolation network of discrete and selective protein-protein interactions. Here, we describe detailed kinetic measurements of the phase transition, along with coarse-grained model simulations, that reveal that LAT condensation is kinetically frustrated by the availability of bonds to form the network. Unlike typical miscibility transitions in which compact domains may coexist at equilibrium, the LAT condensates are dynamically arrested in extended states, kinetically trapped out of equilibrium. Modeling identifies the structural basis for this kinetic arrest as the formation of spindle arrangements, favored by limited multivalent binding interactions along the flexible, intrinsically disordered LAT protein. These results reveal how local factors controlling the kinetics of LAT condensation enable formation of different, stable condensates, which may ultimately coexist within the cell.
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Registered trials
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