Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis.

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Serval ID
serval:BIB_B45BCB6BAFBA
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis.
Journal
Cell Stress and Chaperones
Author(s)
Finka A., Goloubinoff P.
ISSN
1466-1268 (Electronic)
ISSN-L
1355-8145
Publication state
Published
Issued date
2013
Volume
18
Number
5
Pages
591-605
Language
english
Abstract
In the crowded environment of human cells, folding of nascent polypeptides and refolding of stress-unfolded proteins is error prone. Accumulation of cytotoxic misfolded and aggregated species may cause cell death, tissue loss, degenerative conformational diseases, and aging. Nevertheless, young cells effectively express a network of molecular chaperones and folding enzymes, termed here "the chaperome," which can prevent formation of potentially harmful misfolded protein conformers and use the energy of adenosine triphosphate (ATP) to rehabilitate already formed toxic aggregates into native functional proteins. In an attempt to extend knowledge of chaperome mechanisms in cellular proteostasis, we performed a meta-analysis of human chaperome using high-throughput proteomic data from 11 immortalized human cell lines. Chaperome polypeptides were about 10 % of total protein mass of human cells, half of which were Hsp90s and Hsp70s. Knowledge of cellular concentrations and ratios among chaperome polypeptides provided a novel basis to understand mechanisms by which the Hsp60, Hsp70, Hsp90, and small heat shock proteins (HSPs), in collaboration with cochaperones and folding enzymes, assist de novo protein folding, import polypeptides into organelles, unfold stress-destabilized toxic conformers, and control the conformal activity of native proteins in the crowded environment of the cell. Proteomic data also provided means to distinguish between stable components of chaperone core machineries and dynamic regulatory cochaperones.
Pubmed
Web of science
Open Access
Yes
Create date
21/05/2013 13:12
Last modification date
01/10/2019 6:19
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