Cargando…
USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation
Physiological adaptation to proteotoxic stress in the endoplasmic reticulum (ER) requires retrotranslocation of misfolded proteins into the cytoplasm for ubiquitination and elimination by ER-associated degradation (ERAD). A surprising paradox emerging from recent studies is that ubiquitin ligases (E...
Autores principales: | Liu, Yanfen, Soetandyo, Nia, Lee, Jin-gu, Liu, Liping, Xu, Yue, Clemons, William M, Ye, Yihong |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3889402/ https://www.ncbi.nlm.nih.gov/pubmed/24424410 http://dx.doi.org/10.7554/eLife.01369 |
Ejemplares similares
-
gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum
por: Zhang, Ting, et al.
Publicado: (2015) -
The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and Hrd1
por: Menzies, Sam A, et al.
Publicado: (2018) -
Deubiquitinase USP13 maintains glioblastoma stem cells by antagonizing FBXL14-mediated Myc ubiquitination
por: Fang, Xiaoguang, et al.
Publicado: (2017) -
Chaperone gp96 mediates ER-α36 cell membrane expression
por: Hou, Junwei, et al.
Publicado: (2015) -
Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
por: Lee, Jin-Gu, et al.
Publicado: (2013)