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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-3-27
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pubmed:abstractText |
The N-terminus of regulator of G protein signaling 7 (RGS7) contains a dishevelled/egl-10/pleckstrin (DEP) domain of unknown function. To gain insight into its function, we used yeast two-hybrid analysis to screen a human whole brain cDNA library in order to identify proteins that interact specifically with the N-terminus of human RGS7 (amino acid residues 1-248). From this analysis, we identified snapin, a protein associated with the SNARE complex in neurons, as an interactor with the N-terminus of RGS7. Deletion mutation analysis in yeast demonstrated that the interaction between RGS7 and snapin is specific and is mediated primarily by amino acid residues 1-69 of RGS7 (which contains the proximal portion of the DEP domain). The interaction between RGS7 and snapin was also demonstrated in mammalian cells by coimmunoprecipitation and pull-down assays. Our results suggest that RGS7 could play a role in synaptic vesicle exocytosis through its interaction with snapin.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RGS7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNAPIN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
303
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
594-9
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pubmed:dateRevised |
2008-5-7
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pubmed:meshHeading |
pubmed-meshheading:12659861-Animals,
pubmed-meshheading:12659861-Base Sequence,
pubmed-meshheading:12659861-Binding Sites,
pubmed-meshheading:12659861-CHO Cells,
pubmed-meshheading:12659861-Carrier Proteins,
pubmed-meshheading:12659861-Cloning, Molecular,
pubmed-meshheading:12659861-Cricetinae,
pubmed-meshheading:12659861-DNA Primers,
pubmed-meshheading:12659861-GTP-Binding Proteins,
pubmed-meshheading:12659861-Humans,
pubmed-meshheading:12659861-Membrane Proteins,
pubmed-meshheading:12659861-Neuropeptides,
pubmed-meshheading:12659861-Peptide Fragments,
pubmed-meshheading:12659861-RGS Proteins,
pubmed-meshheading:12659861-Recombinant Proteins,
pubmed-meshheading:12659861-Saccharomyces cerevisiae,
pubmed-meshheading:12659861-Signal Transduction,
pubmed-meshheading:12659861-Transfection,
pubmed-meshheading:12659861-Vesicular Transport Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Snapin interacts with the N-terminus of regulator of G protein signaling 7.
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pubmed:affiliation |
Neuroscience Discovery Research, Wyeth Research, Princeton, NJ 08543-8000, USA.
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pubmed:publicationType |
Journal Article
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