English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/113853
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Molecular basis of gephyrin clustering at inhibitory synapses: Role of G- and E-domain interactions

AuthorsSaiyed, Taslimarif; Paarmann, Ingo; Schmitt, Bertram; Haeger, Svenja; Solà, Maria ; Schmalzing, Günther; Weissenhorn, Winfried; Betz, Heinrich
KeywordsGephyrin clustering
Gephyrin scaffolds
Postsynaptic gephyrin clusters
Bifunctional modular proteins
Issue Date23-Feb-2007
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 282(8): 5625-5632 (2007)
AbstractGephyrin 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.
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M610290200
URIhttp://hdl.handle.net/10261/113853
DOI10.1074/jbc.M610290200
Identifiersdoi: 10.1074/jbc.M610290200
issn: 0021-9258
Appears in Collections:(IBMB) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.