Unknown

Dataset Information

0

Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis In Aging Cells.


ABSTRACT: Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the utilization of damaged or needless proteins. Eventually, aging cells, in parallel to the accumulation of flawed proteins, gradually lose their proteostasis mechanisms, and this loss leads to the degeneration of large cellular masses and to number of age-associated pathologies and ultimately death. In this review, we describe the function of proteostasis mechanisms with an emphasis on the possible associations between them.

SUBMITTER: Margulis B 

PROVIDER: S-EPMC7291254 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis In Aging Cells.

Margulis Boris B   Tsimokha Anna A   Zubova Svetlana S   Guzhova Irina I  

Cells 20200524 5


Throughout their life cycles, cells are subject to a variety of stresses that lead to a compromise between cell death and survival. Survival is partially provided by the cell proteostasis network, which consists of molecular chaperones, a ubiquitin-proteasome system of degradation and autophagy. The cooperation of these systems impacts the correct function of protein synthesis/modification/transport machinery starting from the adaption of nascent polypeptides to cellular overcrowding until the u  ...[more]

Similar Datasets

| S-EPMC8164034 | biostudies-literature
| S-EPMC6006194 | biostudies-literature
| S-EPMC2063486 | biostudies-other
| S-EPMC3889881 | biostudies-literature
| S-EPMC6361847 | biostudies-literature
| S-EPMC5954431 | biostudies-literature
| S-EPMC3398549 | biostudies-other
| S-EPMC190409 | biostudies-other