Antigen presentation: Peptides and proteins scramble for the exit

Current Biology

Volumn 10, Issue 22, 2000, Pages

  Lehner, Paul J ^a   Hewitt, Eric W ^a   Römisch, Karin ^a  

^a ADDENBROOKE S HOSPITAL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0034676279     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00793-4     Document Type: Review

References (23)

1. Mechanisms of MHC class I-restricted antigen processing
2. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
3. Function of the transport complex TAP in cellular immune recognition
4. TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective
5. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
6. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
7. Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator
8. Setting the standards: Quality control in the secretory pathway
9. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
10. Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane
11. The translocon: A dynamic gateway at the ER membrane
12. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
13. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
14. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
15. Toxin entry: Retrograde transport through the secretory pathway
16. Cholera toxin is exported from microsomes by the Sec61p complex
17. Ricin A chain utilises the endoplasmic reticulum-associated protein degradation pathway to enter the cytosol of yeast
18. The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane
19. Novel peptide-binding proteins and peptide transport in normal and TAP-deficient microsomes
20. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
21. Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum
22. ER protein quality control and proteasome-mediated protein degradation
23. Getting the UPR hand on misfolded proteins