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.
References
45
Referenced
35
10.1074/jbc.270.34.19873
10.1074/jbc.273.34.22037
10.1074/jbc.274.5.2616
10.1016/S0960-9822(98)70387-2
10.1084/jem.179.2.533
10.1084/jem.180.5.1591
10.1016/1074-7613(95)90090-X
10.1002/j.1460-2075.1995.tb00292.x
10.1016/S0959-4388(98)80068-8
10.1128/MCB.16.9.4700
10.1073/pnas.89.15.7227
10.1242/jcs.112.23.4185
10.1038/384432a0
10.1093/emboj/16.15.4540
10.1038/42276
10.1074/jbc.271.41.25590
10.1002/j.1460-2075.1996.tb00492.x
10.1038/349806a0
10.1016/0092-8674(95)90077-2
10.1016/S0092-8674(00)81861-9
10.1083/jcb.132.3.291
10.1091/mbc.9.12.3455
10.1083/jcb.109.6.2641
10.1091/mbc.3.2.129
10.1083/jcb.147.7.1443
10.1083/jcb.122.1.79
10.1016/0076-6879(91)94004-V
10.1016/S0960-9822(02)00484-0
10.1073/pnas.94.13.6730
10.1002/j.1460-2075.1993.tb05699.x
10.1083/jcb.126.4.925
10.1016/S0092-8674(00)81403-8
10.1002/j.1460-2075.1996.tb00411.x
10.1073/pnas.88.10.4453
10.1002/eji.1830270944
10.1111/j.1432-1033.1997.t01-1-00037.x
10.1093/emboj/17.4.927
10.1074/jbc.275.2.801
10.1093/emboj/18.6.1506
10.1083/jcb.131.6.1377
10.1083/jcb.123.6.1355
10.1016/S0092-8674(00)80767-9
10.1073/pnas.92.21.9643
10.1074/jbc.274.6.3453
10.1038/353726a0
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) |
@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} }