Source:http://linkedlifedata.com/resource/pubmed/id/10373486
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
1999-7-15
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pubmed:databankReference | |
pubmed:abstractText |
The mammalian caveolin gene family consists of caveolins-1, -2, and -3. The expression of caveolin-3 is muscle-specific. In contrast, caveolins-1 and -2 are co-expressed, and they form a hetero-oligomeric complex in many cell types, with particularly high levels in adipocytes, endothelial cells, and fibroblasts. These caveolin hetero-oligomers are thought to represent the functional assembly units that drive caveolae formation in vivo. Here, we investigate the mechanism by which caveolins-1 and -2 form hetero-oligomers. We reconstituted this reciprocal interaction in vivo and in vitro using a variety of complementary approaches, including the generation of glutathione S-transferase fusion proteins and synthetic peptides. Taken together, our results indicate that the membrane-spanning domains of both caveolins-1 and -2 play a critical role in mediating their ability to interact with each other. This is the first demonstration that these unusual membrane-spanning regions found in the caveolin family play a specific role in protein-protein interactions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cav1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18721-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10373486-3T3 Cells,
pubmed-meshheading:10373486-Amino Acid Sequence,
pubmed-meshheading:10373486-Animals,
pubmed-meshheading:10373486-COS Cells,
pubmed-meshheading:10373486-Caveolin 1,
pubmed-meshheading:10373486-Caveolin 2,
pubmed-meshheading:10373486-Caveolins,
pubmed-meshheading:10373486-Cell Membrane,
pubmed-meshheading:10373486-Cloning, Molecular,
pubmed-meshheading:10373486-DNA, Complementary,
pubmed-meshheading:10373486-Epitope Mapping,
pubmed-meshheading:10373486-Membrane Proteins,
pubmed-meshheading:10373486-Mice,
pubmed-meshheading:10373486-Molecular Sequence Data,
pubmed-meshheading:10373486-Open Reading Frames,
pubmed-meshheading:10373486-Protein Conformation,
pubmed-meshheading:10373486-Protein Structure, Secondary
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pubmed:year |
1999
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pubmed:articleTitle |
The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo.
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pubmed:affiliation |
Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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