Glycoprotein degradation: Do sugars hold the key?

Current Biology

Volumn 10, Issue 18, 2000, Pages

  Frigerio, Lorenzo ^a   Lord, J Michael ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0034699356     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00680-1     Document Type: Review

References (17)

1. Setting the standards: Quality control in the secretory pathway
2. Pivotal role of calnexin and mannose trimming in regulating the ER-associated degradation of MHC class I heavy chain
3. Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways
4. Quality control in the secretory pathway
5. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
6. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
7. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
8. Cytosolic degradation of T-cell receptor chains by the proteasome
9. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
10. ER quality control: The cytoplasmic connection
11. Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein
12. Degradation of stearoyl-coenzyme A desaturase: Endoproteolytic cleavage by an integral membrane protease
13. Degradation of HMG-CoA reductase in vitro. Cleavage in the membrane domain by a membrane-bound cysteine protease
14. Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein
15. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
16. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
17. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: The role of N-linked glycans and the unfolded protein response