Cellular and Molecular Life Sciences CMLS

, Volume 63, Issue 7, pp 939–948

Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity

Authors

    • Department of BiochemistryUniversity of Lausanne
    • Laboratory of AIDS immunopathogenesisCentre Hospitalier Universitaire Vaudois
  • F. C. Bender
    • Department of BiochemistryUniversity of Lausanne
    • Department of Microbiology, School of Dental MedicineUniversity of Pennsylvania
  • D. Hess
    • Friedrich Miescher-Institute
  • J. Hofsteenge
    • Friedrich Miescher-Institute
  • C. Bron
    • Department of BiochemistryUniversity of Lausanne
Research Article

DOI: 10.1007/s00018-005-5551-z

Cite this article as:
Doucey, M.-., Bender, F.C., Hess, D. et al. Cell. Mol. Life Sci. (2006) 63: 939. doi:10.1007/s00018-005-5551-z

Abstract.

We report that caveolin-1, one of the major structural protein of caveolae, interacts with TCP-1, a hetero-oligomeric chaperone complex present in all eukaryotic cells that contributes mainly to the folding of actin and tubulin. The caveolin-TCP-1 interaction entails the first 32 amino acids of the N-terminal segment of caveolin. Our data show that caveolin-1 expression is needed for the induction of TCP-1 actin folding function in response to insulin stimulation. Caveolin-1 phosphorylation at tyrosine residue 14 induces the dissociation of caveolin-1 from TCP-1 and activates actin folding. We show that the mechanism by which caveolin-1 modulates TCP-1 activity is indirect and involves the cytoskeleton linker filamin. Filamin is known to bind caveolin-1 and to function as a negative regulator of insulin-mediated signaling. Our data support the notion that the caveolin-filamin interaction contributes to restore insulin-mediated phosphorylation of caveolin, thus allowing the release of active TCP-1.

Keywords.

CaveolinTCP-1foldinginsulinfilaminchaperone

Copyright information

© Birkhäuser Verlag, Basel 2006