Linked Life Data

12682051

Source:http://linkedlifedata.com/resource/pubmed/id/12682051

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2003-6-16
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23046-54
pubmed:dateRevised
2007-5-1
pubmed:meshHeading
pubmed-meshheading:12682051-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:12682051-Amino Acid Sequence, pubmed-meshheading:12682051-Animals, pubmed-meshheading:12682051-Cytoplasm, pubmed-meshheading:12682051-DNA Primers, pubmed-meshheading:12682051-Genes, Reporter, pubmed-meshheading:12682051-Green Fluorescent Proteins, pubmed-meshheading:12682051-Humans, pubmed-meshheading:12682051-Luminescent Proteins, pubmed-meshheading:12682051-Membrane Proteins, pubmed-meshheading:12682051-Mice, pubmed-meshheading:12682051-Molecular Sequence Data, pubmed-meshheading:12682051-Polymerase Chain Reaction, pubmed-meshheading:12682051-R-SNARE Proteins, pubmed-meshheading:12682051-Recombinant Fusion Proteins, pubmed-meshheading:12682051-Sequence Alignment, pubmed-meshheading:12682051-Sequence Homology, Amino Acid, pubmed-meshheading:12682051-Signal Transduction, pubmed-meshheading:12682051-Subcellular Fractions, pubmed-meshheading:12682051-Transfection, pubmed-meshheading:12682051-trans-Golgi Network
pubmed:year
2003
pubmed:articleTitle
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.
pubmed:affiliation
Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Singapore.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't