The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Hop, also known as Stip1 or Sti1, facilitates substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Characterization of proteostasis-related pathways in STIP1 knock-out cell lines reveals that in eukaryotes Stip1 modulates the balance between protein folding and degradation.
Guardado en:
Autores principales: | Kaushik Bhattacharya, Lorenz Weidenauer, Tania Morán Luengo, Ellis C. Pieters, Pablo C. Echeverría, Lilia Bernasconi, Diana Wider, Yashar Sadian, Margreet B. Koopman, Matthieu Villemin, Christoph Bauer, Stefan G. D. Rüdiger, Manfredo Quadroni, Didier Picard |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Honey bee sHSP are responsive to diverse proteostatic stresses and potentially promising biomarkers of honey bee stress
por: Samantha R. Shih, et al.
Publicado: (2021) -
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding
por: Mark R. Woodford, et al.
Publicado: (2016) -
Local unfolding of the HSP27 monomer regulates chaperone activity
por: T. Reid Alderson, et al.
Publicado: (2019) -
The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse.
por: Iwona Grad, et al.
Publicado: (2010) -
The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70
por: Conrado C. Gonçalves, et al.
Publicado: (2021)