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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1996-8-27
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pubmed:abstractText |
VIP21-caveolin is one of the components which form the cytoplasmic surface of caveolae. In vivo, this integral membrane protein is found in homo-oligomers with molecular masses of approximately 200, 400 and 600 kDa. These oligomers are also formed by the addition of cytosol to the in vitro synthesized and membrane inserted VIP21-caveolin. Here we show that long chain fatty acyl coenzyme A esters can completely substitute for cytosol in inducing 200 kDa and 400 kDa complexes, whereas 25-hydroxy-cholesterol can produce the 200 kDa oligomer. In order to understand whether acylation of VIP21-caveolin itself is a prerequisite for oligomerization, we studied a mutant protein lacking all three cysteines. When analyzed by velocity sucrose gradient centrifugation in the presence of the non-ionic detergent octylglucoside, both palmitoylated and non-palmitoylated VIP21-caveolin formed oligomers that were indistinguishable. However, only the oligomers of the non-palmitoylated protein are disrupted when analyzed by SDS-PAGE without boiling. These data suggest that the protein domains of VIP21-caveolin are the primary determinants of oligomerization, but that palmitoylation of cysteine residues can increase the stability of the oligomers.
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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/25-hydroxycholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/CAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxycholesterols,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acids
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
388
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
143-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8690074-Acyl Coenzyme A,
pubmed-meshheading:8690074-Acylation,
pubmed-meshheading:8690074-Animals,
pubmed-meshheading:8690074-Carrier Proteins,
pubmed-meshheading:8690074-Caveolin 1,
pubmed-meshheading:8690074-Caveolins,
pubmed-meshheading:8690074-Cell Line,
pubmed-meshheading:8690074-Cysteine,
pubmed-meshheading:8690074-Dogs,
pubmed-meshheading:8690074-Humans,
pubmed-meshheading:8690074-Hydroxycholesterols,
pubmed-meshheading:8690074-Membrane Proteins,
pubmed-meshheading:8690074-Palmitic Acid,
pubmed-meshheading:8690074-Palmitic Acids
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pubmed:year |
1996
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pubmed:articleTitle |
Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol.
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pubmed:affiliation |
Department of Cell Biology, Max-Delbrück Centre for Molecular Medicine, Berlin-Buch, Germany.
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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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