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Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity.

Science (New York, N.Y.) | Nov 13, 1998

Glycine receptors are anchored at inhibitory chemical synapses by a cytoplasmic protein, gephyrin. Molecular cloning revealed the similarity of gephyrin to prokaryotic and invertebrate proteins essential for synthesizing a cofactor required for activity of molybdoenzymes. Gene targeting in mice showed that gephyrin is required both for synaptic clustering of glycine receptors in spinal cord and for molybdoenzyme activity in nonneural tissues. The mutant phenotype resembled that of humans with hereditary molybdenum cofactor deficiency and hyperekplexia (a failure of inhibitory neurotransmission), suggesting that gephyrin function may be impaired in both diseases.

Pubmed ID: 9812897 RIS Download

Mesh terms: Animals | Animals, Newborn | Brain | Carrier Proteins | Chimera | Coenzymes | Gene Targeting | Glycine | Humans | Membrane Proteins | Metalloproteins | Mice | Molybdenum | Motor Neurons | Oxidoreductases Acting on Sulfur Group Donors | Phenotype | Pteridines | Receptor Aggregation | Receptors, Glycine | Spinal Cord | Stem Cells | Synapses | Synaptic Transmission | Xanthine Dehydrogenase

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