Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Peptides and misfolded secretory proteins are transported efficiently from the endoplasmic reticulum (ER) lumen to the cytosol, where the proteins are degraded by proteasomes. Protein export depends on Sec61p, the ribosome-binding core component of the protein translocation channel in the ER membrane. We found that prebinding of ribosomes abolished export of a glycopeptide from yeast microsomes. Deletion of SSH1, which encodes a ribosome-binding Sec61p homologue in the ER, had no effect on glycopeptide export. A collection of cold-sensitive sec61 mutants displayed a variety of phenotypes: two mutants strongly defective in misfolded protein export from the ER, sec61-32 and sec61-41 , displayed only minor peptide export defects. Glycopeptide export was severely impaired, however, in several sec61 mutants that were only marginally defective in misfolded protein export. In addition, a mutation in SEC63 strongly reduced peptide export from the ER. ER-luminal ATP was required for both misfolded protein and glycopeptide export. We conclude that the protein translocation channel in the ER membrane mediates glycopeptide transport across the ER membrane.

Bibliography

Gillece, P., Pilon, M., & Römisch, K. (2000). The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane. Proceedings of the National Academy of Sciences, 97(9), 4609–4614.

Dates
Type When
Created 23 years ago (July 26, 2002, 10:38 a.m.)
Deposited 3 years, 4 months ago (April 12, 2022, 5:24 p.m.)
Indexed 1 year, 1 month ago (July 21, 2024, 4:30 p.m.)
Issued 25 years, 4 months ago (April 11, 2000)
Published 25 years, 4 months ago (April 11, 2000)
Published Online 25 years, 4 months ago (April 11, 2000)
Published Print 25 years, 3 months ago (April 25, 2000)
Funders 0

None

@article{Gillece_2000, title={The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.090083497}, DOI={10.1073/pnas.090083497}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Gillece, Pauline and Pilon, Marinus and Römisch, Karin}, year={2000}, month=apr, pages={4609–4614} }