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A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments
The central channel Tom40 of the preprotein translocase of outer membrane (TOM) complex is thought to be responsible for the import of virtually all preproteins synthesized outside the mitochondria. In this study, we analyze the topogenesis of the peripheral benzodiazepine receptor (PBR), which inte...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373507/ https://www.ncbi.nlm.nih.gov/pubmed/18158327 http://dx.doi.org/10.1083/jcb.200702143 |
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author | Otera, Hidenori Taira, Yohsuke Horie, Chika Suzuki, Yurina Suzuki, Hiroyuki Setoguchi, Kiyoko Kato, Hiroki Oka, Toshihiko Mihara, Katsuyoshi |
author_facet | Otera, Hidenori Taira, Yohsuke Horie, Chika Suzuki, Yurina Suzuki, Hiroyuki Setoguchi, Kiyoko Kato, Hiroki Oka, Toshihiko Mihara, Katsuyoshi |
author_sort | Otera, Hidenori |
collection | PubMed |
description | The central channel Tom40 of the preprotein translocase of outer membrane (TOM) complex is thought to be responsible for the import of virtually all preproteins synthesized outside the mitochondria. In this study, we analyze the topogenesis of the peripheral benzodiazepine receptor (PBR), which integrates into the mitochondrial outer membrane (MOM) through five hydrophobic transmembrane segments (TMSs) and functions in cholesterol import into the inner membrane. Analyses of in vitro and in vivo import into TOM component–depleted mitochondria reveal that PBR import (1) depends on the import receptor Tom70 but requires neither the Tom20 and Tom22 import receptors nor the import channel Tom40, (2) shares the post-Tom70 pathway with the C-tail–anchored proteins, and (3) requires factors of the mitochondrial intermembrane space. Furthermore, membrane integration of mitofusins and mitochondrial ubiquitin ligase, the MOM proteins with two and four TMSs, respectively, proceeds through the same initial pathway. These findings reveal a previously unidentified pathway of the membrane integration of MOM proteins with multiple TMSs. |
format | Text |
id | pubmed-2373507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-23735072008-06-30 A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments Otera, Hidenori Taira, Yohsuke Horie, Chika Suzuki, Yurina Suzuki, Hiroyuki Setoguchi, Kiyoko Kato, Hiroki Oka, Toshihiko Mihara, Katsuyoshi J Cell Biol Research Articles The central channel Tom40 of the preprotein translocase of outer membrane (TOM) complex is thought to be responsible for the import of virtually all preproteins synthesized outside the mitochondria. In this study, we analyze the topogenesis of the peripheral benzodiazepine receptor (PBR), which integrates into the mitochondrial outer membrane (MOM) through five hydrophobic transmembrane segments (TMSs) and functions in cholesterol import into the inner membrane. Analyses of in vitro and in vivo import into TOM component–depleted mitochondria reveal that PBR import (1) depends on the import receptor Tom70 but requires neither the Tom20 and Tom22 import receptors nor the import channel Tom40, (2) shares the post-Tom70 pathway with the C-tail–anchored proteins, and (3) requires factors of the mitochondrial intermembrane space. Furthermore, membrane integration of mitofusins and mitochondrial ubiquitin ligase, the MOM proteins with two and four TMSs, respectively, proceeds through the same initial pathway. These findings reveal a previously unidentified pathway of the membrane integration of MOM proteins with multiple TMSs. The Rockefeller University Press 2007-12-31 /pmc/articles/PMC2373507/ /pubmed/18158327 http://dx.doi.org/10.1083/jcb.200702143 Text en Copyright © 2007, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Otera, Hidenori Taira, Yohsuke Horie, Chika Suzuki, Yurina Suzuki, Hiroyuki Setoguchi, Kiyoko Kato, Hiroki Oka, Toshihiko Mihara, Katsuyoshi A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title | A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title_full | A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title_fullStr | A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title_full_unstemmed | A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title_short | A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
title_sort | novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373507/ https://www.ncbi.nlm.nih.gov/pubmed/18158327 http://dx.doi.org/10.1083/jcb.200702143 |
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