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  Organization of the native ribosome-translocon complex at the mammalian endoplasmic reticulum membrane

Pfeffer, S., Dudek, J., Zimmermann, R., & Förster, F. (2016). Organization of the native ribosome-translocon complex at the mammalian endoplasmic reticulum membrane. Biochimica et Biophysica Acta-General Subjects, 1860(10), 2122-2129. doi:10.1016/j.bbagen.2016.06.024.

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 Creators:
Pfeffer, Stefan1, Author              
Dudek, Johanna2, Author
Zimmermann, Richard2, Author
Förster, Friedrich1, Author              
Affiliations:
1Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
2external, ou_persistent22              

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Free keywords: SIGNAL RECOGNITION PARTICLE; PROTEIN-QUALITY CONTROL; X-RAY-STRUCTURE; N-GLYCOSYLATION; CONDUCTING CHANNEL; SEC61 TRANSLOCON; ER MEMBRANE; YEAST; OLIGOSACCHARYLTRANSFERASE; SUBSTRATEBiochemistry & Molecular Biology; Biophysics; Ribosome; Endoplasmic reticulum; Protein translocon; Membrane protein biogenesis; Structural biology;
 Abstract: Background: In eukaryotic cells, many proteins have to be transported across or inserted into the endoplasmic reticulum membrane during their biogenesis on the ribosome. This process is facilitated by the protein translocon, a highly dynamic multi-subunit membrane protein complex. Scope of review: The aim of this review is to summarize the current structural knowledge about protein translocon components in mammals. Major conclusions: Various structural biology approaches have been used in synergy to characterize the translocon in recent years. X-ray crystallography and cryoelectron microscopy single particle analysis have yielded highly detailed insights into the structure and functional mechanism of the protein-conducting channel Sec61, which constitutes the functional core of the translocon. Cryoelectron tomography and subtomogram analysis have advanced our understanding of the overall structure, molecular organization and compositional heterogeneity of the translocon in a native membrane environment. Tomography densities at subnanometer resolution revealed an intricate network of interactions between the ribosome, Sec61 and accessory translocon components that assist in protein transport, membrane insertion and maturation. General significance: The protein translocon is a gateway for approximately one third of all synthesized proteins and numerous human diseases are associated with malfunctioning of its components. Thus, detailed insights into the structure and molecular organization of the translocon will not only advance our understanding of membrane protein biogenesis in general, but they can potentially pave the way for novel therapeutic approaches against human diseases. (C) 2016 Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
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Project name : FO 716/3-1 and GRK1721 to FF
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Funding organization : German Research Council

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Title: Biochimica et Biophysica Acta-General Subjects
  Other : Biochim. Biophys. Acta-Gen. Subj.
Source Genre: Journal
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Publ. Info: New York, NY : Elsevier
Pages: - Volume / Issue: 1860 (10) Sequence Number: - Start / End Page: 2122 - 2129 Identifier: ISSN: 0304-4165
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_2