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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2003-7-3
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pubmed:abstractText |
Analysis of membrane protein interactions is difficult because of the hydrophobic nature of these proteins, which often renders conventional biochemical and genetic assays fruitless. This is a substantial problem because proteins that are integral or associated with membranes represent approximately one-third of all proteins in a typical eukaryotic cell. We have shown previously that the modified split-ubiquitin system can be used as a genetic assay for the in vivo detection of interactions between the two characterized yeast transmembrane proteins, Ost1p and Wbp1p. This so-called split-ubiquitin membrane yeast two-hybrid (YTH) system uses the split-ubiquitin approach in which reconstitution of two ubiquitin halves is mediated by a protein-protein interaction. Here we converted the split-ubiquitin membrane YTH system into a generally applicable in vivo screening approach to identify interacting partners of a particular mammalian transmembrane protein. We have demonstrated the effectiveness of this approach by using the mammalian ErbB3 receptor as bait and have identified three previously unknown ErbB3-interacting proteins. In addition, we have confirmed one of the newly found interactions between ErbB3 and the membrane-associated RGS4 protein by coimmunoprecipitating the two proteins from human cells. We expect the split-ubiquitin membrane YTH technology to be valuable for the identification of potential interacting partners of integral membrane proteins from many model organisms.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-10436009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-10683744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-10688190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-10880430,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-11283351,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-11602604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-11792827,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-12223533,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-9576926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-9660808,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12840049-9950680
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1088-9051
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1744-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12840049-Amino Acid Sequence,
pubmed-meshheading:12840049-Animals,
pubmed-meshheading:12840049-Base Sequence,
pubmed-meshheading:12840049-Brain,
pubmed-meshheading:12840049-Cell Line,
pubmed-meshheading:12840049-Cloning, Molecular,
pubmed-meshheading:12840049-DNA, Complementary,
pubmed-meshheading:12840049-Gene Library,
pubmed-meshheading:12840049-Genetic Vectors,
pubmed-meshheading:12840049-Humans,
pubmed-meshheading:12840049-Kidney,
pubmed-meshheading:12840049-Macromolecular Substances,
pubmed-meshheading:12840049-Membrane Proteins,
pubmed-meshheading:12840049-Molecular Sequence Data,
pubmed-meshheading:12840049-Peptide Mapping,
pubmed-meshheading:12840049-Protein Interaction Mapping,
pubmed-meshheading:12840049-RGS Proteins,
pubmed-meshheading:12840049-Rats,
pubmed-meshheading:12840049-Receptor, erbB-3,
pubmed-meshheading:12840049-Saccharomyces cerevisiae,
pubmed-meshheading:12840049-Two-Hybrid System Techniques,
pubmed-meshheading:12840049-Ubiquitin
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pubmed:year |
2003
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pubmed:articleTitle |
Identification of novel ErbB3-interacting factors using the split-ubiquitin membrane yeast two-hybrid system.
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pubmed:affiliation |
Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich-Irchel, CH-8057 Zurich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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