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


Journal Article

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.

Full Text

Cited Authors

  • Feng, G; Tintrup, H; Kirsch, J; Nichol, MC; Kuhse, J; Betz, H; Sanes, JR

Published Date

  • November 1998

Published In

Volume / Issue

  • 282 / 5392

Start / End Page

  • 1321 - 1324

PubMed ID

  • 9812897

Pubmed Central ID

  • 9812897

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.282.5392.1321


  • eng