Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Dorit Hanein; Kent E.S. Matlack; Berit Jungnickel; Kathrin Plath; Kai Uwe Kalies; Kenneth R. Miller; Tom A. Rapoport; Christopher W. Akey

doi:10.1016/S0092-8674(00)81391-4

Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Dorit Hanein^*, Kent E.S. Matlack, Berit Jungnickel, Kathrin Plath, Kai Uwe Kalies, Kenneth R. Miller, Tom A. Rapoport, Christopher W. Akey

^*Corresponding author for this work

Institute of Biology

283 Citations (Scopus)

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 ~85Å and a central pore of ~20 Å. 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 post-translational transport.

Original language	English
Journal	Cell
Volume	87
Issue number	4
Pages (from-to)	721-732
Number of pages	12
ISSN	0092-8674
DOIs	https://doi.org/10.1016/S0092-8674(00)81391-4
Publication status	Published - 15.01.1996

Funding

This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript.

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Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/S0092-8674(00)81391-4

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title = "Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation",

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 \textasciitilde{}85{\AA} and a central pore of \textasciitilde{}20 {\AA}. 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 post-translational transport.",

author = "Dorit Hanein and Matlack, \{Kent E.S.\} and Berit Jungnickel and Kathrin Plath and Kalies, \{Kai Uwe\} and Miller, \{Kenneth R.\} and Rapoport, \{Tom A.\} and Akey, \{Christopher W.\}",

note = "Funding Information: This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",

year = "1996",

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doi = "10.1016/S0092-8674(00)81391-4",

language = "English",

volume = "87",

pages = "721--732",

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T1 - Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

AU - Hanein, Dorit

AU - Matlack, Kent E.S.

AU - Jungnickel, Berit

AU - Plath, Kathrin

AU - Kalies, Kai Uwe

AU - Miller, Kenneth R.

AU - Rapoport, Tom A.

AU - Akey, Christopher W.

N1 - Funding Information: This work was supported by NIH grants to C. W. A. and T. A. R., the Fulbright Junior Research Program (D. H.), and a Rothschild Fellowship (D. H.). We thank Dr. J. Wall and M. Simon for collecting scanning-transmission electron microscopy images analyzed in this work, and Dr. E. Bullitt for help with the Brandeis mass-analysis programs. We thank M. Rolls, P. Stein, and E. Hartmann for critical reading of the manuscript. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 1996/1/15

Y1 - 1996/1/15

N2 - 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 ~85Å and a central pore of ~20 Å. 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 post-translational transport.

AB - 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 ~85Å and a central pore of ~20 Å. 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 post-translational transport.

UR - https://www.scopus.com/pages/publications/0345444027

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M3 - Journal articles

C2 - 8929540

AN - SCOPUS:0345444027

SN - 0092-8674

VL - 87

SP - 721

EP - 732

JO - Cell

JF - Cell

IS - 4

ER -

Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Abstract

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