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

Doucey, M. ; Bender, F. ; Hess, D. ; Hofsteenge, J. ; Bron, C.

In: Cellular and Molecular Life Sciences CMLS, 2006, vol. 63, no. 7-8, p. 939-948

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    Titre
    • Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity
    Auteur
    • Doucey, M.. Department of Biochemistry, University of Lausanne, chemin des Boveresses 155, 1066, Epalinges, Switzerland
    • Bender, F.. Department of Biochemistry, University of Lausanne, chemin des Boveresses 155, 1066, Epalinges, Switzerland
    • Hess, D.. Friedrich Miescher-Institute, P.O. Box 2543, 4002, Basel, Switzerland
    • Hofsteenge, J.. Friedrich Miescher-Institute, P.O. Box 2543, 4002, Basel, Switzerland
    • Bron, C.. Department of Biochemistry, University of Lausanne, chemin des Boveresses 155, 1066, Epalinges, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Cellular and Molecular Life Sciences CMLS, 2006, vol. 63, no. 7-8, p. 939-948. Birkhäuser-Verlag; www.birkhauser.ch
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:317724
    Summary
    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