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http://purl.uniprot.org/citations/17254016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17254016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17254016http://www.w3.org/2000/01/rdf-schema#comment"A mechanism for regulating the strength of synaptic inhibition is enabled by altering the number of GABA(A) receptors available at the cell surface. Clathrin and adaptor protein 2 (AP2) complex-mediated endocytosis is known to play a fundamental role in regulating cell surface GABA(A) receptor numbers. Very recently, we have elucidated that phospholipase C-related catalytically inactive protein (PRIP) molecules are involved in the phosphorylation-dependent regulation of the internalization of GABA(A) receptors through association with receptor beta subunits and protein phosphatases. In this study, we examined the implications of PRIP molecules in clathrin-mediated constitutive GABA(A) receptor endocytosis, independent of phospho-regulation. We performed a constitutive receptor internalization assay using human embryonic kidney 293 (HEK293) cells transiently expressed with GABA(A) receptor alpha/beta/gamma subunits and PRIP. PRIP was internalized together with GABA(A) receptors, and the process was inhibited by PRIP-binding peptide which blocks PRIP binding to beta subunits. The clathrin heavy chain, mu2 and beta2 subunits of AP2 and PRIP-1, were complexed with GABA(A) receptor in brain extract as analyzed by co-immunoprecipitation assay using anti-PRIP-1 and anti-beta2/3 GABA(A) receptor antibody or by pull-down assay using beta subunits of GABA(A) receptor. These results indicate that PRIP is primarily implicated in the constitutive internalization of GABA(A) receptor that requires clathrin and AP2 protein complex."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.org/dc/terms/identifier"doi:10.1111/j.1471-4159.2006.04399.x"xsd:string
http://purl.uniprot.org/citations/17254016http://purl.org/dc/terms/identifier"doi:10.1111/j.1471-4159.2006.04399.x"xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Fujii M."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Fujii M."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Hirata M."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Hirata M."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Moss S.J."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Moss S.J."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Kittler J.T."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Kittler J.T."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Mizokami A."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Mizokami A."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Kanematsu T."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Kanematsu T."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Nabekura J."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/author"Nabekura J."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/pages"898-905"xsd:string
http://purl.uniprot.org/citations/17254016http://purl.uniprot.org/core/pages"898-905"xsd:string