Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity.
Data(s) |
2006
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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 |