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Título: | Molecular basis of gephyrin clustering at inhibitory synapses: Role of G- and E-domain interactions |
Autor: | Saiyed, Taslimarif; Paarmann, Ingo; Schmitt, Bertram; Haeger, Svenja; Solà, Maria CSIC ORCID ; Schmalzing, Günther; Weissenhorn, Winfried; Betz, Heinrich | Palabras clave: | Gephyrin clustering Gephyrin scaffolds Postsynaptic gephyrin clusters Bifunctional modular proteins |
Fecha de publicación: | 23-feb-2007 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 282(8): 5625-5632 (2007) | Resumen: | Gephyrin is a bifunctional modular protein that, in neurons, clusters glycine receptors and γ-aminobutyric acid, type A receptors in the postsynaptic membrane of inhibitory synapses. By x-ray crystallography and cross-linking, the N-terminal G-domain of gephyrin has been shown to form trimers and the C-terminal E-domain dimers, respectively. Gephyrin therefore has been proposed to form a hexagonal submembranous lattice onto which inhibitory receptors are anchored. Here, crystal structure-based substitutions at oligomerization interfaces revealed that both G-domain trimerization and E-domain dimerization are essential for the formation of higher order gephyrin oligomers and postsynaptic gephyrin clusters. Insertion of the alternatively spliced C5′ cassette into the G-domain inhibited clustering by interfering with trimerization, and mutation of the glycine receptor β-subunit binding region prevented the localization of the clusters at synaptic sites. Together our findings show that domain interactions mediate gephyrin scaffold formation. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc. | Versión del editor: | http://dx.doi.org/10.1074/jbc.M610290200 | URI: | http://hdl.handle.net/10261/113853 | DOI: | 10.1074/jbc.M610290200 | Identificadores: | doi: 10.1074/jbc.M610290200 issn: 0021-9258 |
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