Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking.

@article{Uittenbogaard1998CharacterizationOA,
  title={Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking.},
  author={Annette M. Uittenbogaard and Yun-shu Ying and Eric J. Smart},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 11},
  pages={6525-32}
}
Caveolin is a 22-kDa protein that appears to play a critical role in regulating the cholesterol concentration of caveolae. Even though caveolin is thought to be a membrane protein, several reports suggest that this peculiar protein can traffic independently of membrane vesicles. We now present evidence that a cytosolic pool of caveolin is part of a heat-shock protein-immunophilin chaperone complex consisting of caveolin, heat-shock protein 56, cyclophilin 40, cyclophilin A, and cholesterol… CONTINUE READING
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