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http://purl.uniprot.org/citations/9024696http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9024696http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9024696http://www.w3.org/2000/01/rdf-schema#comment"The molecular mechanisms underlying the organization of ion channels and signaling molecules at the synaptic junction are largely unknown. Recently, members of the PSD-95/SAP90 family of synaptic MAGUK (membrane-associated guanylate kinase) proteins have been shown to interact, via their NH2-terminal PDZ domains, with certain ion channels (NMDA receptors and K+ channels), thereby promoting the clustering of these proteins. Although the function of the NH2-terminal PDZ domains is relatively well characterized, the function of the Src homology 3 (SH3) domain and the guanylate kinase-like (GK) domain in the COOH-terminal half of PSD-95 has remained obscure. We now report the isolation of a novel synaptic protein, termed GKAP for guanylate kinase-associated protein, that binds directly to the GK domain of the four known members of the mammalian PSD-95 family. GKAP shows a unique domain structure and appears to be a major constituent of the postsynaptic density. GKAP colocalizes and coimmunoprecipitates with PSD-95 in vivo, and coclusters with PSD-95 and K+ channels/NMDA receptors in heterologous cells. Given their apparent lack of guanylate kinase enzymatic activity, the fact that the GK domain can act as a site for protein-protein interaction has implications for the function of diverse GK-containing proteins (such as p55, ZO-1, and LIN-2/CASK)."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.org/dc/terms/identifier"doi:10.1083/jcb.136.3.669"xsd:string
http://purl.uniprot.org/citations/9024696http://purl.org/dc/terms/identifier"doi:10.1083/jcb.136.3.669"xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Hsueh Y.-P."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Hsueh Y.-P."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Rao A."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Rao A."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Craig A.M."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Craig A.M."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Rothschild A."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Rothschild A."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Naisbitt S."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/author"Naisbitt S."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/pages"669-678"xsd:string
http://purl.uniprot.org/citations/9024696http://purl.uniprot.org/core/pages"669-678"xsd:string