Cargando…
Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation
The endoplasmic reticulum (ER) maintains an environment essential for secretory protein folding. Consequently, the premature transport of polypeptides would be harmful to the cell. To avert this scenario, mechanisms collectively termed “ER quality control” prevent the transport of nascent polypeptid...
Autores principales: | Spear, Eric D., Ng, Davis T.W. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2005
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171888/ https://www.ncbi.nlm.nih.gov/pubmed/15809311 http://dx.doi.org/10.1083/jcb.200411136 |
Ejemplares similares
-
Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
por: Vashist, Shilpa, et al.
Publicado: (2004) -
N‐glycan processing selects ERAD‐resistant misfolded proteins for ER‐to‐lysosome‐associated degradation
por: Fregno, Ilaria, et al.
Publicado: (2021) -
The glycan‐dependent ERAD machinery degrades topologically diverse misfolded proteins
por: Shin, Yun‐Ji, et al.
Publicado: (2018) -
The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum
por: Zhang, Jianjun, et al.
Publicado: (2021) -
A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation
por: Hüttner, Silvia, et al.
Publicado: (2014)