| pubmed-article:9658161 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9658161 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:9658161 | lifeskim:mentions | umls-concept:C0148339 | lld:lifeskim |
| pubmed-article:9658161 | lifeskim:mentions | umls-concept:C1513342 | lld:lifeskim |
| pubmed-article:9658161 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
| pubmed-article:9658161 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9658161 | pubmed:dateCreated | 1999-1-22 | lld:pubmed |
| pubmed-article:9658161 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9658161 | pubmed:abstractText | Screening of a library derived from primary human endothelial cells revealed a novel human isoform of vesicle-associated membrane protein-1 (VAMP-1), a protein involved in the targeting and/or fusion of transport vesicles to their target membrane. We have termed this novel isoform VAMP-1B and designated the previously described isoform VAMP-1A. VAMP-1B appears to be an alternatively spliced form of VAMP-1. A similar rat splice variant of VAMP-1 (also termed VAMP-1B) has recently been reported. Five different cultured cell lines, from different lineages, all contained VAMP-1B but little or no detectable VAMP-1A mRNA, as assessed by PCR. In contrast, brain mRNA contained VAMP-1A but no VAMP-1B. The VAMP-1B sequence encodes a protein identical to VAMP-1A except for the carboxy-terminal five amino acids. VAMP-1 is anchored in the vesicle membrane by a carboxy-terminal hydrophobic sequence. In VAMP-1A the hydrophobic anchor is followed by a single threonine, which is the carboxy-terminal amino acid. In VAMP-1B the predicted hydrophobic membrane anchor is shortened by four amino acids, and the hydrophobic sequence is immediately followed by three charged amino acids, arginine-arginine-aspartic acid. Transfection of human endothelial cells with epitope-tagged VAMP-1B demonstrated that VAMP-1B was targeted to mitochondria whereas VAMP-1A was localized to the plasma membrane and endosome-like structures. Analysis of C-terminal mutations of VAMP-1B demonstrated that mitochondrial targeting depends both on the addition of positive charge at the C terminus and a shortened hydrophobic membrane anchor. These data suggest that mitochondria may be integrated, at least at a mechanistic level, to the vesicular trafficking pathways that govern protein movement between other organelles of the cell. | lld:pubmed |
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| pubmed-article:9658161 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9658161 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9658161 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9658161 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9658161 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9658161 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:9658161 | pubmed:author | pubmed-author:GambleJJ | lld:pubmed |
| pubmed-article:9658161 | pubmed:author | pubmed-author:VadasMM | lld:pubmed |
| pubmed-article:9658161 | pubmed:author | pubmed-author:WattenbergB... | lld:pubmed |
| pubmed-article:9658161 | pubmed:author | pubmed-author:IsenmannSS | lld:pubmed |
| pubmed-article:9658161 | pubmed:author | pubmed-author:Khew-GoodallY... | lld:pubmed |
| pubmed-article:9658161 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9658161 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:9658161 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9658161 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9658161 | pubmed:pagination | 1649-60 | lld:pubmed |
| pubmed-article:9658161 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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