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


Autoria(s): Doucey M.A.; Bender F.C.; Hess D.; Hofsteenge J.; Bron C.
Data(s)

2006

Resumo

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.

Identificador

http://serval.unil.ch/?id=serval:BIB_83E496BD7B59

isbn:1420-682X[print], 1420-682X[linking]

pmid:16568240

doi:10.1007/s00018-005-5551-z

isiid:000237359800017

Idioma(s)

en

Fonte

Cellular and Molecular Life Sciences, vol. 63, no. 7-8, pp. 939-948

Palavras-Chave #Amino Acid Sequence; Caveolin 1/metabolism; Cell Line; Chaperonin Containing TCP-1; Chaperonins/drug effects; Chaperonins/metabolism; HT29 Cells; Humans; Insulin/pharmacology; Molecular Sequence Data; Multiprotein Complexes/metabolism; Phosphorylation; Protein Folding; Signal Transduction
Tipo

info:eu-repo/semantics/article

article