Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum
Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R.
American Association for the Advancement of Science (AAAS)
Published 2018
American Association for the Advancement of Science (AAAS)
Published 2018
| Publication Date: |
2018-04-13
|
|---|---|
| Publisher: |
American Association for the Advancement of Science (AAAS)
|
| Print ISSN: |
0036-8075
|
| Electronic ISSN: |
1095-9203
|
| Topics: |
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
|
| Keywords: |
Biochemistry, Cell Biology
|
| Published by: |
| _version_ | 1836398891273027584 |
|---|---|
| autor | Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. |
| beschreibung | Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo–electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. |
| citation_standardnr | 6233638 |
| datenlieferant | ipn_articles |
| feed_id | 25 |
| feed_publisher | American Association for the Advancement of Science (AAAS) |
| feed_publisher_url | http://www.aaas.org/ |
| insertion_date | 2018-04-13 |
| journaleissn | 1095-9203 |
| journalissn | 0036-8075 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | American Association for the Advancement of Science (AAAS) |
| quelle | Science |
| relation | http://science.sciencemag.org/cgi/content/short/360/6385/215?rss=1 |
| schlagwort | Biochemistry, Cell Biology |
| search_space | articles |
| shingle_author_1 | Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. |
| shingle_author_2 | Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. |
| shingle_author_3 | Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. |
| shingle_author_4 | Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. |
| shingle_catch_all_1 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum Biochemistry, Cell Biology Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo–electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_2 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum Biochemistry, Cell Biology Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo–electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_3 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum Biochemistry, Cell Biology Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo–electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_catch_all_4 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum Biochemistry, Cell Biology Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo–electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., Beckmann, R. American Association for the Advancement of Science (AAAS) 0036-8075 00368075 1095-9203 10959203 |
| shingle_title_1 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| shingle_title_2 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| shingle_title_3 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| shingle_title_4 | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| timestamp | 2025-06-30T23:34:17.262Z |
| titel | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| titel_suche | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum |
| topic | W V TE-TZ SQ-SU WW-YZ TA-TD U |
| uid | ipn_articles_6233638 |