Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum

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