Small heat-shock proteins and their role in mechanical stress.
Cell Stress Chaperones
; 25(4): 601-613, 2020 07.
Article
en En
| MEDLINE
| ID: mdl-32253742
ABSTRACT
The ability of cells to respond to stress is central to health. Stress can damage folded proteins, which are vulnerable to even minor changes in cellular conditions. To maintain proteostasis, cells have developed an intricate network in which molecular chaperones are key players. The small heat-shock proteins (sHSPs) are a widespread family of molecular chaperones, and some sHSPs are prominent in muscle, where cells and proteins must withstand high levels of applied force. sHSPs have long been thought to act as general interceptors of protein aggregation. However, evidence is accumulating that points to a more specific role for sHSPs in protecting proteins from mechanical stress. Here, we briefly introduce the sHSPs and outline the evidence for their role in responses to mechanical stress. We suggest that sHSPs interact with mechanosensitive proteins to regulate physiological extension and contraction cycles. It is likely that further study of these interactions - enabled by the development of experimental methodologies that allow protein contacts to be studied under the application of mechanical force - will expand our understanding of the activity and functions of sHSPs, and of the roles played by chaperones in general.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Estrés Mecánico
/
Proteínas de Choque Térmico Pequeñas
/
Proteostasis
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Cell Stress Chaperones
Año:
2020
Tipo del documento:
Article
País de afiliación:
Estados Unidos