Cargando…
Disulfide-crosslink analysis of the ubiquitin ligase Hrd1 complex during endoplasmic reticulum-associated protein degradation
Misfolded proteins in the lumen of the endoplasmic reticulum (ER) are retrotranslocated into the cytosol and degraded by the ubiquitin-proteasome system, a pathway termed luminal ER-associated protein degradation. Retrotranslocation is mediated by a conserved protein complex, consisting of the ubiqu...
Autores principales: | Pisa, Rudolf, Rapoport, Tom A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9478403/ https://www.ncbi.nlm.nih.gov/pubmed/35970394 http://dx.doi.org/10.1016/j.jbc.2022.102373 |
Ejemplares similares
-
Cycles of autoubiquitination and deubiquitination regulate the ERAD ubiquitin ligase Hrd1
por: Peterson, Brian G, et al.
Publicado: (2019) -
Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling: Transmembrane Control of Hrd1p by Hrd3p
por: Gardner, Richard G., et al.
Publicado: (2000) -
Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase
por: Rubenstein, Eric M., et al.
Publicado: (2012) -
gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum
por: Zhang, Ting, et al.
Publicado: (2015) -
Putative Interaction Proteins of the Ubiquitin Ligase Hrd1 in
Magnaporthe oryzae
por: Jiang, Haolang, et al.
Publicado: (2018)