Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities

• Published in: Proceedings of the National Academy of Sciences - PNAS 2011-07, Vol.108 (29), p.12113-12118
• Main Authors: Silva, John-Paul, Lelianova, Vera G, Ermolyuk, Yaroslav S, Vysokov, Nickolai, Hitchen, Paul G, Berninghausen, Otto, Rahman, M. Atiqur, Zangrandi, Alice, Fidalgo, Sara, Tonevitsky, Alexander G, Dell, Anne, Volynski, Kirill E, Ushkaryov, Yuri A
• Format: Article
• Language: English
• Subjects: adhesion; Animals; Axons; Base Sequence; Biological Sciences; Brain; calcium; calcium signaling; Calcium Signaling - physiology; Cells; Cloning, Molecular; coculture; Coculture techniques; G-protein coupled receptors; Hippocampus - metabolism; Hippocampus - physiology; Immunoblotting; Ligands; microscopy; Microscopy, Immunoelectron; molecular cloning; Molecular Sequence Data; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Neurons; Neurotransmitters; Proteins; Rats; Receptors; Receptors, Cell Surface - genetics; Receptors, Cell Surface - metabolism; Receptors, Peptide - metabolism; Sequence Analysis, DNA; Signal transduction; surface interactions; Synapses; Synapses - metabolism; synaptic transmission; Synaptic Transmission - physiology; synaptogenesis
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.1019434108

Latrophilin 1 (LPH1), a neuronal receptor of α-latrotoxin, is implicated in neurotransmitter release and control of presynaptic Ca²⁺. 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