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http://purl.uniprot.org/citations/28972156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28972156http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28972156http://www.w3.org/2000/01/rdf-schema#comment"ClC-4 is an intracellular Cl-/H+ exchanger that is highly expressed in the brain and whose dysfunction has been linked to intellectual disability and epilepsy. Here we studied the subcellular localization of human ClC-4 in heterologous expression systems. ClC-4 is retained in the endoplasmic reticulum (ER) upon overexpression in HEK293T cells. Co-expression with distinct ClC-3 splice variants targets ClC-4 to late endosome/lysosomes (ClC-3a and ClC-3b) or recycling endosome (ClC-3c). When expressed in cultured astrocytes, ClC-4 sorted to endocytic compartments in WT cells but was retained in the ER in Clcn3-/- cells. To understand the virtual absence of ER-localized ClC-4 in WT astrocytes, we performed association studies by high-resolution clear native gel electrophoresis. Although other CLC channels and transporters form stable dimers, ClC-4 was mostly observed as monomer, with ClC-3-ClC-4 heterodimers being more stable than ClC-4 homodimers. We conclude that unique oligomerization properties of ClC-4 permit regulated targeting of ClC-4 to various endosomal compartment systems via expression of different ClC-3 splice variants."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m117.801951"xsd:string
http://purl.uniprot.org/citations/28972156http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m117.801951"xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Fahlke C."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Fahlke C."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Bungert-Pluemke S."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Bungert-Pluemke S."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Franzen A."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Franzen A."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Guzman R.E."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/author"Guzman R.E."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/pages"19055-19065"xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/pages"19055-19065"xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/title"Preferential association with ClC-3 permits sorting of ClC-4 into endosomal compartments."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/title"Preferential association with ClC-3 permits sorting of ClC-4 into endosomal compartments."xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/28972156http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/28972156http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28972156
http://purl.uniprot.org/citations/28972156http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28972156