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http://purl.uniprot.org/citations/16957052http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16957052http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16957052http://www.w3.org/2000/01/rdf-schema#comment"The formation of transport vesicles that bud from endoplasmic reticulum (ER) exit sites is dependent on the COPII coat made up of three components: the small GTPase Sar1, the Sec23/24 complex, and the Sec13/31 complex. Here, we provide evidence that apoptosis-linked gene 2 (ALG-2), a Ca(2+)-binding protein of unknown function, regulates the COPII function at ER exit sites in mammalian cells. ALG-2 bound to the Pro-rich region of Sec31A, a ubiquitously expressed mammalian orthologue of yeast Sec31, in a Ca(2+)-dependent manner and colocalized with Sec31A at ER exit sites. A Ca(2+) binding-deficient ALG-2 mutant, which did not bind Sec31A, lost the ability to localize to ER exit sites. Overexpression of the Pro-rich region of Sec31A or RNA interference-mediated Sec31A depletion also abolished the ALG-2 localization at these sites. In contrast, depletion of ALG-2 substantially reduced the level of Sec31A associated with the membrane at ER exit sites. Finally, treatment with a cell-permeable Ca(2+) chelator caused the mislocalization of ALG-2, which was accompanied by a reduced level of Sec31A at ER exit sites. We conclude that ALG-2 is recruited to ER exit sites via Ca(2+)-dependent interaction with Sec31A and in turn stabilizes the localization of Sec31A at these sites."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e06-05-0444"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e06-05-0444"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Komada M."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Komada M."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Tani K."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Kitamura N."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Kitamura N."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Yamasaki A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/author"Yamasaki A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/pages"4876-4887"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/pages"4876-4887"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/title"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/title"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/16957052http://purl.uniprot.org/core/volume"17"xsd:string