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http://purl.uniprot.org/citations/15615712http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15615712http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15615712http://www.w3.org/2000/01/rdf-schema#comment"Memapsin 2 (BACE, beta-secretase) is a membrane-associated aspartic protease that initiates the hydrolysis of beta-amyloid precursor protein (APP) leading to the production of amyloid-beta (A beta) and the progression of Alzheimer disease. Both memapsin 2 and APP are transported from the cell surface to endosomes where APP is cleaved by memapsin 2. We described previously that the cytosolic domain of memapsin 2 contains an acid cluster-dileucine motif (ACDL) that binds the VHS (Vps-27, Hrs, and STAM) domain of Golgi-localized gamma-ear-containing ARF-binding (GGA) proteins (He, X., Zhu, G., Koelsch, G., Rodgers, K. K., Zhang, X. C., and Tang, J. (2003) Biochemistry 42, 12174-12180). Here we report that GGA proteins colocalize in the trans-Golgi network and endosomes with memapsin 2 and a memapsin 2 chimera containing a cytosolic domain of a mannose-6-phosphate receptor. Depleting cellular GGA proteins with RNA interference or mutation of serine 498 to stop the phosphorylation of ACDL resulted in the accumulation of memapsin 2 in early endosomes. A similar change of memapsin 2 localization also was observed when a retromer subunit, VPS26, was depleted. These observations suggest that GGA proteins function with the phosphorylated ACDL in the memapsin 2-recycling pathway from endosomes to trans-Golgi on the way back to the cell surface."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411296200"xsd:string
http://purl.uniprot.org/citations/15615712http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411296200"xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"He X."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"He X."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Chang W.P."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/author"Chang W.P."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/pages"11696-11703"xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/pages"11696-11703"xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/title"GGA proteins mediate the recycling pathway of memapsin 2 (BACE)."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/title"GGA proteins mediate the recycling pathway of memapsin 2 (BACE)."xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15615712http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15615712http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15615712
http://purl.uniprot.org/citations/15615712http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15615712