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

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  • 2006-03-29
Published in:
  • Cellular and molecular life sciences : CMLS. - 2006
Amino Acid Sequence
Caveolin 1
Cell Line
Chaperonin Containing TCP-1
Chaperonins
HT29 Cells
Humans
Insulin
Molecular Sequence Data
Multiprotein Complexes
Phosphorylation
Protein Folding
Signal Transduction
English 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.
Language
  • English
Open access status
green
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Persistent URL
https://sonar.ch/global/documents/98840
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