Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational Diseases
نویسندگان
چکیده
منابع مشابه
Roles of ubiquitin in endoplasmic reticulum-associated protein degradation (ERAD).
In the secretory pathway, quality control for the correct folding of proteins is largely occurring in the endoplasmic reticulum (ER), at the earliest possible stage and in an environment where early folding intermediates mix with terminally misfolded species. An elaborate cellular mechanism aims at dividing the former from the latter and promotes the selective transport of misfolded species bac...
متن کاملRegulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin
Quality control of protein folding inside the endoplasmic reticulum (ER) includes chaperone-mediated assistance in folding and the selective targeting of terminally misfolded species to a pathway called ER-associated protein degradation, or simply ERAD. Once selected for ERAD, substrates will be transported (back) into the cytosol, a step called retrotranslocation. Although still ill defined, r...
متن کاملSpecific degradation of proteins within the secretory pathway
Background: The endoplasmic reticulumassociated degradation (ERAD) is a cellular mechanism to eliminate misfolded proteins. Results: Fusion of a target-binding domain to a fragment of the ERAD-associated protein SEL1L induces specific degradation of secretory and membrane-bound target proteins. Conclusion: The new recombinant proteins (degradins) efficiently induce degradation of targets within...
متن کاملMolecular functions of the ubiquitin domain protein Herp in Synoviolin mediated endoplasmic reticulum associated protein degradation (ERAD)
.......................................................................................................................................4 ZUSAMMENFASSUNG ......................................................................................................................5
متن کاملEndoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins.
The serpinopathies are a family of diseases characterized by the accumulation of ordered polymers of mutant protein within the endoplasmic reticulum. They are a diverse group including alpha(1)-antitrypsin deficiency and the inherited dementia familial encephalopathy with neuroserpin inclusion bodies or FENIB. We have used transient transfection of COS7 cells and mouse embryonic fibroblasts, PC...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Cold Spring Harbor Perspectives in Biology
سال: 2019
ISSN: 1943-0264
DOI: 10.1101/cshperspect.a033928