ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
Sanchón et al find that misfolded proteins formed in the ER can become associated with mitochondria, both in mammalian cells and in yeast, resulting in impaired mitochondrial function. They further discover that components of ERMES-mediated ER-mitochondria contacts are needed for this mechanism, whi...
Guardado en:
Autores principales: | Adrián Cortés Sanchón, Harshitha Santhosh Kumar, Matilde Mantovani, Ivan Osinnii, José María Mateos, Andres Kaech, Dimitri Shcherbakov, Rashid Akbergenov, Erik C. Böttger |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/bf08851619654161a435709327ef2900 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
por: Sophia Ungelenk, et al.
Publicado: (2016) -
ER-mitochondria contacts promote mtDNA nucleoids active transportation via mitochondrial dynamic tubulation
por: Jinshan Qin, et al.
Publicado: (2020) -
Miro clusters regulate ER-mitochondria contact sites and link cristae organization to the mitochondrial transport machinery
por: Souvik Modi, et al.
Publicado: (2019) -
Silencing of the ER and Integrative Stress Responses in the Liver of Mice with Error-Prone Translation
por: James Moore, et al.
Publicado: (2021) -
Cellular senescence links mitochondria-ER contacts and aging
por: Dorian V. Ziegler, et al.
Publicado: (2021)