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http://purl.uniprot.org/citations/17196169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17196169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17196169http://www.w3.org/2000/01/rdf-schema#comment"Intracellular localization of the penta-EF-hand Ca2+-binding protein ALG-2 in HeLa cells was investigated by immunofluorescent confocal microscopy using a polyclonal antibody. In addition to its presence in the nucleus, ALG-2 was found to be distributed in a punctate pattern in the cytoplasm, where it was partly co-stained with an endoplasmic reticulum (ER) exit site marker p125. In vitro GST pull down analysis demonstrated that ALG-2 and its alternatively spliced isoform interact with the COPII component Sec31A in a Ca2+-dependent manner, and a biotin-labeled ALG-2 overlay assay revealed direct binding of ALG-2 to Sec31A. Biochemical and immunofluorescent microscopic analyses showed that ALG-2 was enriched at the Sec31A-localizing membrane compartments upon stimulation with the Ca2+ ionophore A23187. In contrast, treatment of cells with the membrane-permeant Ca2+ chelator BAPTA-AM led to a dispersion of ALG-2 throughout the cells and to a significant loss of Sec31A in the perinuclear region. These findings establish Sec31A as a novel target for ALG-2 and provide a framework for studies on the roles of ALG-2 in ER-Golgi transport."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.12.101"xsd:string
http://purl.uniprot.org/citations/17196169http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.12.101"xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/pages"756-763"xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/pages"756-763"xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/title"ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/title"ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner."xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/volume"353"xsd:string
http://purl.uniprot.org/citations/17196169http://purl.uniprot.org/core/volume"353"xsd:string
http://purl.uniprot.org/citations/17196169http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17196169
http://purl.uniprot.org/citations/17196169http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17196169