The role of the ubiquitin-proteasome system in ER quality control.
Misfolded endoplasmic reticulum (ER) proteins are eliminated by the retrotranslocation pathway in eukaryotes, which is an important physiological adaptation to ER stress. This pathway can be hijacked by certain viruses to destroy folded cellular proteins, such as MHC class I heavy chain. Recent studies have highlighted the importance of the ubiquitin-proteasome system (UPS) in this process.
Ye
Yihong
Y
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540, USA. yihongy@mail.nih.gov
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000502:physiology*; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D025821:Polyubiquitin / Q000502:physiology; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D017510:Protein Folding; D021381:Protein Transport / Q000502:physiology; D025801:Ubiquitin / Q000502:physiology*; D043743:Ubiquitin-Protein Ligase Complexes / Q000502:physiology; D000074405:Valosin Containing Protein
D018797:Cell Cycle Proteins; D009687:Nuclear Proteins; D025801:Ubiquitin; D025821:Polyubiquitin; D043743:Ubiquitin-Protein Ligase Complexes; D046988:Proteasome Endopeptidase Complex; D000251:Adenosine Triphosphatases; C404942:p97 ATPase; D000074405:Valosin Containing Protein