Fiche du document
2006
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00018-005-5551-z
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/16568240
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pissn/1420-682X[print], 1420-682X[linking]
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_83E496BD7B590
info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer
Sujets proches
Proteins--Folding Folding of proteinsCiter ce document
M.A. Doucey et al., « Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity. », Serveur académique Lausannois, ID : 10.1007/s00018-005-5551-z
Métriques
Partage / Export
Résumé
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.
