Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast.

Détails

ID Serval
serval:BIB_C02DBF9E43FB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast.
Périodique
Molecular and Cellular Biology
Auteur(s)
Jacobson T., Priya S., Sharma S.K., Andersson S., Jakobsson S., Tanghe R., Ashouri A., Rauch S., Goloubinoff P., Christen P., Tamás M.J.
ISSN
1098-5549 (Electronic)
ISSN-L
0270-7306
Statut éditorial
Publié
Date de publication
2017
Peer-reviewed
Oui
Volume
37
Numéro
17
Pages
1-15
Langue
anglais
Résumé
Cadmium is a highly poisonous metal and is classified as a human carcinogen. While its toxicity is undisputed, the underlying in vivo molecular mechanisms are not fully understood. Here, we demonstrate that cadmium induces aggregation of cytosolic proteins in living Saccharomyces cerevisiae cells. Cadmium primarily targets proteins in the process of synthesis or folding, probably by interacting with exposed thiol groups in not-yet-folded proteins. On the basis of in vitro and in vivo data, we show that cadmium-aggregated proteins form seeds that increase the misfolding of other proteins. Cells that cannot efficiently protect the proteome from cadmium-induced aggregation or clear the cytosol of protein aggregates are sensitized to cadmium. Thus, protein aggregation may contribute to cadmium toxicity. This is the first report on how cadmium causes misfolding and aggregation of cytosolic proteins in vivo The proposed mechanism might explain not only the molecular basis of the toxic effects of cadmium but also the suggested role of this poisonous metal in the pathogenesis of certain protein-folding disorders.

Mots-clé
Saccharomyces cerevisiae, cadmium, metal toxicity, protein aggregation, protein degradation, protein folding, zinc
Pubmed
Web of science
Création de la notice
22/06/2017 17:54
Dernière modification de la notice
20/08/2019 16:34
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