ArticleEMBO reports2023
The structure of fly Teneurin-m reveals an asymmetric self-assembly that allows expansion into zippers.
Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- The teneurin TEN-1 and its ligand LRON-11 support microbiota-induced neuroprotection and mechanosensory function in C. elegans.Current biology : CB · 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
- Organic Phototransistor Photonic Synapses for Artificial Vision.Nano-micro letters · 2026Review
- Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026Review
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Reconstitution of synaptic junctions orchestrated by teneurin-latrophilin complexes.Science (New York, N.Y.) · 2025Article
- Article
- Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition.Nature communications · 2024Article
- The structure of fly Teneurin-m reveals an asymmetric self-assembly that allows expansion into zippers.EMBO reports · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Teneurins are conserved cell adhesion molecules essential for embryogenesis and neural development in animals. Key to teneurin function is the ability of its extracellular region to form homophilic interactions in cis and/or in trans. However, our molecular understanding of teneurin homophilic interaction remains largely incomplete. Here, we showed that an extracellular fragment of Teneurin-m, the major teneurin homolog in flies, behaves as a homodimer in solution. The structure of Teneurin-m revealed that the transthyretin-related domain from one protomer and the β-propeller domain from the other mediates Teneurin-m self-association, which is abolished by point mutation of conserved residues. Strikingly, this architecture generates an asymmetric oligomerization interface that enables expansion of Teneurin-m into long zipper arrays reminiscent of protocadherins. An alternatively spliced site that exists only in vertebrates and regulates homophilic interaction in mammalian teneurins overlaps with the fly Teneurin-m self-association interface. Our work provides a molecular understanding of teneurin homophilic interaction and sheds light on its role in teneurin function throughout evolution.
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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.