ArticleProceedings of the National Academy of Sciences of the United States of America2011
Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.
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Who cites it
164 citing papers in PubMed, 251 citations in OpenAlex.
- The teneurin TEN-1 and its ligand LRON-11 support microbiota-induced neuroprotection and mechanosensory function in C. elegans.Current biology : CB · 2026Article
- Disentangling Sex Differences in Sulfonylurea Drug Response With Genome-Wide Association Studies in Individuals With Type 2 Diabetes.Clinical pharmacology and therapeutics · 2026Article
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- Accurate genomic predictions for chronic wasting disease in North American elk.G3 (Bethesda, Md.) · 2026Article
- Molecular continuity between axon guidance and synaptic function.Molecules and cells · 2026Review
- The therapeutic potential of orphan adhesion G-protein-coupled receptors.Nature reviews. Drug discovery · 2026Review
- Adhesion G protein-coupled receptors.Pharmacological reviews · 2026Review
- Latrophilin-1-Mediated GCells · 2026Article
- EndothelialThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Structurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development.Nature communications · 2026Article
- The expanding roles of adhesion GPCRs in neural circuit assembly.Molecules and cells · 2026Review
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Synaptic Cell Adhesion: A Functional Perspective.Advances in neurobiology · 2026Review
- Adhesion G-Protein Coupled Receptors in Neurological and Psychiatric Disorders.Journal of psychiatry and brain science · 2025Article
- The Mechanism of LTXInternational journal of molecular sciences · 2025Article
- Structural basis and functional roles for Toll-like receptor binding to Latrophilin in C. elegans development.Nature structural & molecular biology · 2025Article
- Entorhinal cortex layer III Adgrl2 expression controls topographical circuit connectivity required for sequence learning.Translational psychiatry · 2025Article
- The Dissociation of Latrophilin Fragments by Perfluorooctanoic Acid (PFOA) Inhibits LTXToxins · 2025Article
- Reconstitution of synaptic junctions orchestrated by teneurin-latrophilin complexes.Science (New York, N.Y.) · 2025Article
104 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
Abstract
Latrophilin 1 (LPH1), a neuronal receptor of α-latrotoxin, is implicated in neurotransmitter release and control of presynaptic Ca(2+). As an "adhesion G-protein-coupled receptor," LPH1 can convert cell surface interactions into intracellular signaling. To examine the physiological functions of LPH1, we used LPH1's extracellular domain to purify its endogenous ligand. A single protein of ∼275 kDa was isolated from rat brain and termed Lasso. Peptide sequencing and molecular cloning have shown that Lasso is a splice variant of teneurin-2, a brain-specific orphan cell surface receptor with a function in neuronal pathfinding and synaptogenesis. We show that LPH1 and Lasso interact strongly and specifically. They are always copurified from rat brain extracts. Coculturing cells expressing LPH1 with cells expressing Lasso leads to their mutual attraction and formation of multiple junctions to which both proteins are recruited. Cells expressing LPH1 form chimerical synapses with hippocampal neurons in cocultures; LPH1 and postsynaptic neuronal protein PSD-95 accumulate on opposite sides of these structures. Immunoblotting and immunoelectron microscopy of purified synapses and immunostaining of cultured hippocampal neurons show that LPH1 and Lasso are enriched in synapses; in both systems, LPH1 is presynaptic, whereas Lasso is postsynaptic. A C-terminal fragment of Lasso interacts with LPH1 and induces Ca(2+) signals in presynaptic boutons of hippocampal neurons and in neuroblastoma cells expressing LPH1. Thus, LPH1 and Lasso can form transsynaptic complexes capable of inducing presynaptic Ca(2+) signals, which might affect synaptic functions.
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