Latrophilins function as heterophilic cell-adhesion molecules by binding to teneurins: regulation by alternative splicing

• Published in: The Journal of biological chemistry Vol. 289; no. 1; pp. 387 - 402
• Main Authors: Boucard, Antony A, Maxeiner, Stephan, Südhof, Thomas C
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 03.01.2014
• Subjects: Alternative Splicing - physiology; Animals; Cell Adhesion - physiology; Drosophila melanogaster; Drosophila Proteins - chemistry; Drosophila Proteins - genetics; Drosophila Proteins - metabolism; HEK293 Cells; Humans; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Neurobiology; Neurons - chemistry; Neurons - cytology; Neurons - metabolism; Protein Binding - physiology; Rats; Receptors, Peptide - chemistry; Receptors, Peptide - genetics; Receptors, Peptide - metabolism; Synapses - chemistry; Synapses - genetics; Synapses - metabolism; Tenascin - chemistry; Tenascin - genetics; Tenascin - metabolism; α-Latrotoxin; Ligand-binding Protein; Synapse Formation; G Protein-coupled Receptors (GPCR); Neurexin; Alternative Splicing; FLRT3; Neurons; Teneurin; Cell Adhesion

Latrophilin-1, -2, and -3 are adhesion-type G protein-coupled receptors that are auxiliary α-latrotoxin receptors, suggesting that they may have a synaptic function. Using pulldowns, we here identify teneurins, type II transmembrane proteins that are also candidate synaptic cell-adhesion molecules,...