ArticleNature chemistry2016
Allosteric activation of membrane-bound glutamate receptors using coordination chemistry within living cells.
Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Light- and chemical-induced ciliary signaling governs dorsal/ventral regionalization of human telencephalic organoids.Nature communications · 2026Article
- N-Acyl-N-Alkyl Sulfonamide Mediated Bioconjugation ofHis-Tag Fused Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Coordination chemogenetics for activation of GPCR-type glutamate receptors in brain tissue.Nature communications · 2022Article
- Chemogenetics of cell surface receptors: beyond genetic and pharmacological approaches.RSC chemical biology · 2022Review
- Orthogonal Activation of Metabotropic Glutamate Receptor Using Coordination Chemogenetics.Frontiers in chemistry · 2021Article
- Organelle membrane-specific chemical labeling and dynamic imaging in living cells.Nature chemical biology · 2020Article
- Chemogenetic Approach Using Ni(II) Complex-Agonist Conjugates Allows Selective Activation of Class A G-Protein-Coupled Receptors.ACS central science · 2018Article
- Review
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Authors and funding
9 authors.
Funding
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Abstract
The controlled activation of proteins in living cells is an important goal in protein-design research, but to introduce an artificial activation switch into membrane proteins through rational design is a significant challenge because of the structural and functional complexity of such proteins. Here we report the allosteric activation of two types of membrane-bound neurotransmitter receptors, the ion-channel type and the G-protein-coupled glutamate receptors, using coordination chemistry in living cells. The high programmability of coordination chemistry enabled two His mutations, which act as an artificial allosteric site, to be semirationally incorporated in the vicinity of the ligand-binding pockets. Binding of Pd(2,2'-bipyridine) at the allosteric site enabled the active conformations of the glutamate receptors to be stabilized. Using this approach, we were able to activate selectively a mutant glutamate receptor in live neurons, which initiated a subsequent signal-transduction pathway.
Indexed as
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Registered trials
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