ArticleNature communications2018
Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Adhesion G protein-coupled receptors.Pharmacological reviews · 2026Review
- The schizophrenia associated protein DISC1 forms a multivalent tetrameric hub via conserved UVR dimers.Nature communications · 2026Article
- Structurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development.Nature communications · 2026Article
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.PLoS pathogens · 2025Article
- Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery.Nature communications · 2024Article
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- Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition.Nature communications · 2024Article
- Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.Nature communications · 2023Article
- The structure of fly Teneurin-m reveals an asymmetric self-assembly that allows expansion into zippers.EMBO reports · 2023Article
- Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission.Nature communications · 2023Article
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- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- A novel role for Teneurin C-terminal Associated Peptide (TCAP) in the regulation of cardiac activity in the Sydney rock oyster,Frontiers in endocrinology · 2023Article
- Distal extracellular teneurin region (teneurin C-terminal associated peptide; TCAP) possesses independent intracellular calcium regulating actions,Biochemistry and biophysics reports · 2022Article
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- Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.Chemical reviews · 2022Review
- Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions.The EMBO journal · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.
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