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| Item Type: | Article |
|---|---|
| Title: | Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol |
| Creators Name: | Monier, S., Dietzen, D.J., Hastings, W.R., Lublin, D.M. and Kurzchalia, T.V. |
| Abstract: | 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. |
| Keywords: | VIP21-Caveolin, Caveolae, Oligomerization, Cholesterol, Fatty Acylation, Animals, Dogs |
| Source: | FEBS Letters |
| ISSN: | 0014-5793 |
| Publisher: | Elsevier |
| Volume: | 388 |
| Number: | 2-3 |
| Page Range: | 143-149 |
| Date: | 17 June 1996 |
| Official Publication: | https://doi.org/10.1016/0014-5793(96)00519-4 |
| PubMed: | View item in PubMed |
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