Cargando…
Inadequate BiP availability defines endoplasmic reticulum stress
How endoplasmic reticulum (ER) stress leads to cytotoxicity is ill-defined. Previously we showed that HeLa cells readjust homeostasis upon proteostatically driven ER stress, triggered by inducible bulk expression of secretory immunoglobulin M heavy chain (μ(s)) thanks to the unfolded protein respons...
Autores principales: | Vitale, Milena, Bakunts, Anush, Orsi, Andrea, Lari, Federica, Tadè, Laura, Danieli, Alberto, Rato, Claudia, Valetti, Caterina, Sitia, Roberto, Raimondi, Andrea, Christianson, John C, van Anken, Eelco |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6417858/ https://www.ncbi.nlm.nih.gov/pubmed/30869076 http://dx.doi.org/10.7554/eLife.41168 |
Ejemplares similares
-
Ratiometric sensing of BiP-client versus BiP levels by the unfolded protein response determines its signaling amplitude
por: Bakunts, Anush, et al.
Publicado: (2017) -
MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP
por: Yan, Yahui, et al.
Publicado: (2019) -
FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP
por: Preissler, Steffen, et al.
Publicado: (2016) -
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum
por: Preissler, Steffen, et al.
Publicado: (2015) -
Iron affects Ire1 clustering propensity and the amplitude of endoplasmic reticulum stress signaling
por: Cohen, Nir, et al.
Publicado: (2017)