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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

Open access
Hanein, Dorit, Matlack, Kent E.S, Jungnickel, Berit, Plath, Kathrin, Kalies, Kai-Uwe, Miller, Kenneth R, Rapoport, Tom A, Akey, Christopher W·1996·Cell

Abstract

The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endoplasmic reticulum (ER) membrane, associating with either ribosomes or the Sec62/63 complex to perform co- and posttranslational transport, respectively. We show by electron microscopy that purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of approximately 85 A and a central pore of approximately 20 A. Each oligomer contains 3-4 heterotrimers. Similar ring structures are seen in reconstituted proteoliposomes and native membranes. Oligomer formation by the reconstituted Sec61p complex is stimulated by its association with ribosomes or the Sec62/63p complex. We propose that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and posttranslational transport.

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Metadata

Authors
Hanein, D., Matlack, K. E. S., Jungnickel, B., Plath, K., Kalies, K.-U., Miller, K. R., Rapoport, T. A., & Akey, C. W.
Venue
Cell
Publisher
Elsevier BV
Published
1996-11
Volume
87
Issue
4
Pages
721-732
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2157729659
Cited by
341
References
0
FWCI
12.75
Type
journal article
Language
en
Open access
hybrid

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Hanein, D., Matlack, K. E. S., Jungnickel, B., Plath, K., Kalies, K.-U., Miller, K. R., Rapoport, T. A., & Akey, C. W. (1996). Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation. Cell. https://doi.org/10.1016/s0092-8674(00)81391-4

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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