Epilepsy-Related Ligand/Receptor Complex LGI1 and ADAM22 Regulate Synaptic Transmission
| Autor: | David S. Bredt, Masaki Fukata, Roger A. Nicoll, Tsuyoshi Iwanaga, Hillel Adesnik, Yuko Fukata |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
medicine.medical_specialty
Receptor complex N-Methylaspartate Recombinant Fusion Proteins Nerve Tissue Proteins AMPA receptor Neurotransmission Biology Ligands Transfection Hippocampus Synaptic Transmission Cell Line Cerebellar Cortex Mice Epilepsy Basic Science Internal medicine medicine Animals Humans Receptors AMPA alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid Cerebral Cortex Multidisciplinary ADAM22 Intracellular Signaling Peptides and Proteins Glutamate receptor Membrane Proteins Proteins medicine.disease Protein Structure Tertiary Rats ADAM Proteins Endocrinology Disks Large Homolog 4 Protein Synapses Intercellular Signaling Peptides and Proteins Calcium Channels Epilepsies Partial Neuroscience Postsynaptic density Protein Binding |
| Zdroj: | Science. 313:1792-1795 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1129947 |
| Popis: | Abnormally synchronized synaptic transmission in the brain causes epilepsy. Most inherited forms of epilepsy result from mutations in ion channels. However, one form of epilepsy, autosomal dominant partial epilepsy with auditory features (ADPEAF), is characterized by mutations in a secreted neuronal protein, LGI1. We show that ADAM22, a transmembrane protein that when mutated itself causes seizure, serves as a receptor for LGI1. LGI1 enhances AMPA receptor-mediated synaptic transmission in hippocampal slices. The mutated form of LGI1 fails to bind to ADAM22. ADAM22 is anchored to the postsynaptic density by cytoskeletal scaffolds containing stargazin. These studies in rat brain indicate possible avenues for understanding human epilepsy. |
| Databáze: | OpenAIRE |
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