Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum
Braunger, Katharina; Pfeffer, Stefan; Shrimal, Shiteshu; Gilmore, Reid; Berninghausen, Otto; Mandon, Elisabet C; Becker, Thomas; Förster, Friedrich; Beckmann, Roland
(2018) Science, volume 360, issue 6385, pp. 215 - 219
(Article)
Abstract
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
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(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.
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Keywords: Cryoelectron Microscopy, Endoplasmic Reticulum, Glycosylation, HEK293 Cells, Hexosyltransferases, Humans, Membrane Proteins, Models, Molecular, Protein Conformation, Protein Transport, Ribosomes, SEC Translocation Channels, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science
Note: Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
(Peer reviewed)
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