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

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Serval ID
serval:BIB_83E496BD7B59
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Caveolin-1 interacts with the chaperone complex TCP-1 and modulates its protein folding activity.
Journal
Cellular and Molecular Life Sciences
Author(s)
Doucey M.A., Bender F.C., Hess D., Hofsteenge J., Bron C.
ISSN
1420-682X[print], 1420-682X[linking]
Publication state
Published
Issued date
2006
Volume
63
Number
7-8
Pages
939-948
Language
english
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.
Keywords
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
Pubmed
Web of science
Open Access
Yes
Create date
28/01/2008 9:28
Last modification date
01/10/2019 7:18
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