Cargando…
Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates
Ubiquitin (Ub) modification of proteins plays a prominent role in the regulation of multiple cell processes, including endoplasmic reticulum–associated degradation (ERAD). Until recently, ubiquitination of substrates was thought to occur only via isopeptide bonds, typically to lysine residues. Sever...
Autores principales: | Wang, Xiaoli, Herr, Roger A., Rabelink, Martijn, Hoeben, Rob C., Wiertz, Emmanuel J.H.J., Hansen, Ted H. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2806592/ https://www.ncbi.nlm.nih.gov/pubmed/19951915 http://dx.doi.org/10.1083/jcb.200908036 |
Ejemplares similares
-
Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
por: Wang, Xiaoli, et al.
Publicado: (2007) -
Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W
por: Davies, Christopher W., et al.
Publicado: (2021) -
UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic exit
por: Garnett, Mathew J., et al.
Publicado: (2009) -
The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER
por: Stagg, Helen R., et al.
Publicado: (2009) -
Quality Control of ER Membrane Proteins by the RNF185/Membralin Ubiquitin Ligase Complex
por: van de Weijer, Michael L., et al.
Publicado: (2020)