ArticleNature structural & molecular biology2021
De novo design of tyrosine and serine kinase-driven protein switches.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Opportunities for artificial intelligence and synthetic biology in designing living drug delivery systems.Advanced drug delivery reviews · 2026Review
- Review
- Enzyme-Free Phosphorylation with Kinetic Gating in a De Novo Coiled-Coil System.Journal of the American Chemical Society · 2026Article
- Mass spectrometry integrates protein design into structural biology method development.QRB discovery · 2026Review
- Article
- A Designed ZnJournal of the American Chemical Society · 2025Article
- How well do contextual protein encodings learn structure, function, and evolutionary context?Cell systems · 2025Article
- Perspectives on Synthetic Protein Circuits in Mammalian Cells.Current opinion in biomedical engineering · 2024Article
- Engineering signalling pathways in mammalian cells.Nature biomedical engineering · 2024Review
- Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code.Nature communications · 2024Article
- Functional and antigenic characterization of SARS-CoV-2 spike fusion peptide by deep mutational scanning.Nature communications · 2024Article
- Expanding Native Mass Spectrometry to the Masses.Journal of the American Society for Mass Spectrometry · 2024Article
- Combining machine learning with structure-based protein design to predict and engineer post-translational modifications of proteins.PLoS computational biology · 2024Article
- Ocean to Tree: Leveraging Single-Molecule RNA-Seq to Repair Genome Gene Models and Improve Phylogenomic Analysis of Gene and Species Evolution.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Functional and antigenic characterization of SARS-CoV-2 spike fusion peptide by deep mutational scanning.bioRxiv : the preprint server for biology · 2023Article
- Engineering synthetic phosphorylation signaling networks in human cells.bioRxiv : the preprint server for biology · 2023Article
- Rational Design of Phosphorylation-Responsive Coiled Coil-Peptide Assemblies.ACS synthetic biology · 2023Article
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
Abstract
Kinases play central roles in signaling cascades, relaying information from the outside to the inside of mammalian cells. De novo designed protein switches capable of interfacing with tyrosine kinase signaling pathways would open new avenues for controlling cellular behavior, but, so far, no such systems have been described. Here we describe the de novo design of two classes of protein switch that link phosphorylation by tyrosine and serine kinases to protein-protein association. In the first class, protein-protein association is required for phosphorylation by the kinase, while in the second class, kinase activity drives protein-protein association. We design systems that couple protein binding to kinase activity on the immunoreceptor tyrosine-based activation motif central to T-cell signaling, and kinase activity to reconstitution of green fluorescent protein fluorescence from fragments and the inhibition of the protease calpain. The designed switches are reversible and function in vitro and in cells with up to 40-fold activation of switching by phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.