Sis1 potentiates the stress response to protein aggregation and elevated temperature

Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease protein in yeast cells and perform a genetic screen...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Courtney L. Klaips, Michael H. M. Gropp, Mark S. Hipp, F. Ulrich Hartl
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Q
Acceso en línea:https://doaj.org/article/bf06109c704f419bbd81a8c23509df78
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
Descripción
Sumario:Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease protein in yeast cells and perform a genetic screen for chaperone factors that allow yeast cells to activate a potent stress response. They identify Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress and further show that both Sis1 and its mammalian homolog DnaJB6 regulate the magnitude of the cellular heat stress response, indicating that this mechanism is conserved.