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http://purl.uniprot.org/citations/8774707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8774707http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8774707http://www.w3.org/2000/01/rdf-schema#comment"Sec1-related proteins are involved in docking and fusion of transport vesicles in eukaryotic cells. Here we report the cloning and molecular characterization of a Sec1-related protein expressed in the MDCK epithelial cell line. This protein represents a canine counterpart of the murine Munc-18-2/Munc-18b/muSec1 protein, displays 93% amino acid identity with these proteins, has a similar tissue mRNA expression pattern, and associates in vitro with syntaxins 1A, 2, and 3. In situ hybridization analysis of embryonic mouse tissues revealed prominent expression of the munc-18-2 mRNA in the epithelia of several tissues. Cell-fractionation studies demonstrated that the majority of Munc-18-2 is membrane associated. Most of the protein is washed off the membranes by sodium carbonate, pH 11.5. However, the protein is poorly solubilized by detergent treatment. The Munc-18-2 protein was localized, by immunofluorescence microscopy, to the plasma membrane of MDCK cells, and is apically distributed in the epithelial cells of mouse tissues. When overexpressed in COS-1 cells, the protein appeared to be largely cytosolic. However, upon expression with syntaxin 1A, it displayed a shift to the plasma membrane, where the two proteins colocalized. These results identified Munc-18-2 as a predominantly epithelial vesicle-transport protein with a polarized distribution and provided novel in vivo evidence for the association of Sec1-related proteins with members of the syntaxin family."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.0638u.x"xsd:string
http://purl.uniprot.org/citations/8774707http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1996.0638u.x"xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Jaentti J."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Jaentti J."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Jansson S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Jansson S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Keraenen S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Keraenen S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Ehnholm C."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Ehnholm C."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Olkkonen V.M."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Olkkonen V.M."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Lehtonen E."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Lehtonen E."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Riento K."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Riento K."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Hielm S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/author"Hielm S."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8774707http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string