Cargando…
ERAD of proteins containing aberrant transmembrane domains requires ubiquitylation of cytoplasmic lysine residues
Clearance of misfolded proteins from the endoplasmic reticulum (ER) is mediated by the ubiquitin-proteasome system in a process known as ER-associated degradation (ERAD). The mechanisms through which proteins containing aberrant transmembrane domains are degraded by ERAD are poorly understood. To ad...
Autores principales: | Briant, Kit, Koay, Yee-Hui, Otsuka, Yuka, Swanton, Eileithyia |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4712780/ https://www.ncbi.nlm.nih.gov/pubmed/26446255 http://dx.doi.org/10.1242/jcs.171215 |
Ejemplares similares
-
Transmembrane domain quality control systems operate at the endoplasmic reticulum and Golgi apparatus
por: Briant, Kit, et al.
Publicado: (2017) -
Restoration of mutant bestrophin-1 expression, localisation and function in a polarised epithelial cell model
por: Uggenti, Carolina, et al.
Publicado: (2016) -
Ubiquitylation in ERAD: Reversing to Go Forward?
por: Tsai, Yien Che, et al.
Publicado: (2011) -
Vaccinia virus virulence factor N1 can be ubiquitylated on multiple lysine residues
por: Maluquer de Motes, Carlos, et al.
Publicado: (2014) -
Non-lysine ubiquitylation: Doing things differently
por: Kelsall, Ian R.
Publicado: (2022)