http://purl.uniprot.org/citations/12682051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12682051 | http://www.w3.org/2000/01/rdf-schema#comment | "SNAREs represent a superfamily of proteins responsible for the last stage of docking and subsequent fusion in diverse intracellular membrane transport events. The Vamp subfamily of SNAREs contains 7 members (Vamp1, Vamp2, Vamp3/cellubrevin, Vamp4, Vamp5, Vamp7/Ti-Vamp, and Vamp8/endobrevin) that are distributed in various post-Golgi structures. Vamp4 and Vamp5 are distributed predominantly in the trans-Golgi network (TGN) and the plasma membrane, respectively. When C-terminally tagged with enhanced green fluorescent protein, the majority of Vamp4 and Vamp5 is correctly targeted to the TGN and plasma membrane, respectively. Swapping the N-terminal cytoplasmic region and the C-terminal membrane anchor domain between Vamp4 and Vamp5 demonstrates that the N-terminal cytoplasmic region of these two SNAREs contains the correct subcellular targeting information. As compared with Vamp5, Vamp4 contains an N-terminal extension of 51 residues. Appending this 51-residue N-terminal extension onto the N terminus of Vamp5 results in targeting of the chimeric protein to the TGN, suggesting that this N-terminal extension of Vamp4 contains a dominant and autonomous targeting signal for the TGN. Analysis of deletion mutants of this N-terminal region suggests that this TGN-targeting signal is encompassed within a smaller region consisting of a di-Leu motif followed by two acidic clusters. The essential role of the di-Leu motif and the second acidic cluster was then established by site-directed mutagenesis."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m303214200"xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/author | "Hong W."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/author | "Zeng Q."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/author | "Tran T.T."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/author | "Tan H.X."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/pages | "23046-23054"xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/title | "The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network."xsd:string |
http://purl.uniprot.org/citations/12682051 | http://purl.uniprot.org/core/volume | "278"xsd:string |
http://purl.uniprot.org/citations/12682051 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12682051 |
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