Endoplasmic-reticulum-associated protein degradation inside and outside of the endoplasmic reticulum |
| |
Authors: | N Erwin Ivessa Claudia Kitzmüller Maddalena de Virgilio |
| |
Institution: | (1) Department of Molecular Genetics, Biocenter Vienna, Dr.-Bohr-Gasse 9/2, A-1030 Vienna, Austria |
| |
Abstract: | Summary Newly synthesized polypeptides that enter the endomembrane system encounter a folding environment in the lumen of the endoplasmic reticulum (ER) constituted by enzymes, lectinlike proteins, and molecular chaperones. The folding process is under scrutiny of this abundant catalytic machinery, and failure of the new arrivals to assume a stable and functional conformation is met with targeting to proteolytic destruction, a process which has been termed ER-associated degradation (ERAD). In recent years it became clear that, in most cases, proteolysis appears to take place in the cytosol after retro-translocation of the substrate proteins from the ER, and to depend on the ubiquitin-proteasome pathway. On the other hand, proteolytic activities within the ER that have been widely neglected so far may also contribute to the turnover of proteins delivered to ERAD. Thus, ERAD is being deciphered as a complex process that requires communication-dependent regulated proteolytic activities within both the ER lumen and the cytosol. Here we discuss some recent findings on ERAD and their implications on possible mechanisms involved.Abbreviations lAT
alpha-1-antitrypsin
- apoB
apolipoprotein B
- BiP
immunoglobulin-heavy-chain-binding protein
- CFTR
cystic fibrosis transmembrane conductance regulator
- CPY
carboxypeptidase Y
- ER
endoplasmic reticulum
- ERAD ER
associated degradation
- HMG-CoA
3-hydroxy-3-methylglutaryl coenzyme A
- MHC
major histocompatibility complex
- PDI
protein disulflde isomerase
- TCR
T cell antigen receptor |
| |
Keywords: | Endoplasmic reticulum Protease Protein degradation Retro-translocation Ubiquitin-proteasome pathway |
本文献已被 SpringerLink 等数据库收录! |
|