Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol

Solange Monier, Dennis J. Dietzen, W. Randall Hastings, Douglas M. Lublin, Teymuras V. Kurzchalia

Research output: Contribution to journalArticlepeer-review

161 Scopus citations


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.

Original languageEnglish
Pages (from-to)143-149
Number of pages7
JournalFEBS Letters
Issue number2-3
StatePublished - Jun 17 1996


  • Caveolae
  • Cholesterol
  • Fatty acylation
  • Oligomerization
  • V1P21-caveolin


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