Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10
The protein Mdm10 is known to be present in the endoplasmic reticulum-mitochondria encounter structure (ERMES) and in mitochondrial sorting and assembly machinery (SAM). Here, the authors examine how this protein interacts with SAM and EMRES, showing that the SAM-mediated protein machinery is indepe...
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| Language: | English |
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Nature Publishing Group
2016-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms13021 |
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doaj-9bf2b01669244292939e16b34fde24892021-05-11T10:35:51ZengNature Publishing GroupNature Communications2041-17232016-10-017111410.1038/ncomms13021Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10Lars Ellenrieder0Łukasz Opaliński1Lars Becker2Vivien Krüger3Oliver Mirus4Sebastian P. Straub5Katharina Ebell6Nadine Flinner7Sebastian B. Stiller8Bernard Guiard9Chris Meisinger10Nils Wiedemann11Enrico Schleiff12Richard Wagner13Nikolaus Pfanner14Thomas Becker15Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgDivision of Biophysics, School of Biology/Chemistry, University of OsnabrückDivision of Biophysics, School of Biology/Chemistry, University of OsnabrückMolecular Cell Biology of Plants, University of FrankfurtInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgDivision of Biophysics, School of Biology/Chemistry, University of OsnabrückMolecular Cell Biology of Plants, University of FrankfurtInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgCentre de Génétique Moléculaire, Centre National de la Recherche ScientifiqueInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgMolecular Cell Biology of Plants, University of FrankfurtDivision of Biophysics, School of Biology/Chemistry, University of OsnabrückInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgInstitute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of FreiburgThe protein Mdm10 is known to be present in the endoplasmic reticulum-mitochondria encounter structure (ERMES) and in mitochondrial sorting and assembly machinery (SAM). Here, the authors examine how this protein interacts with SAM and EMRES, showing that the SAM-mediated protein machinery is independent of ERMES.https://doi.org/10.1038/ncomms13021 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Lars Ellenrieder Łukasz Opaliński Lars Becker Vivien Krüger Oliver Mirus Sebastian P. Straub Katharina Ebell Nadine Flinner Sebastian B. Stiller Bernard Guiard Chris Meisinger Nils Wiedemann Enrico Schleiff Richard Wagner Nikolaus Pfanner Thomas Becker |
| spellingShingle |
Lars Ellenrieder Łukasz Opaliński Lars Becker Vivien Krüger Oliver Mirus Sebastian P. Straub Katharina Ebell Nadine Flinner Sebastian B. Stiller Bernard Guiard Chris Meisinger Nils Wiedemann Enrico Schleiff Richard Wagner Nikolaus Pfanner Thomas Becker Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 Nature Communications |
| author_facet |
Lars Ellenrieder Łukasz Opaliński Lars Becker Vivien Krüger Oliver Mirus Sebastian P. Straub Katharina Ebell Nadine Flinner Sebastian B. Stiller Bernard Guiard Chris Meisinger Nils Wiedemann Enrico Schleiff Richard Wagner Nikolaus Pfanner Thomas Becker |
| author_sort |
Lars Ellenrieder |
| title |
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 |
| title_short |
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 |
| title_full |
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 |
| title_fullStr |
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 |
| title_full_unstemmed |
Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10 |
| title_sort |
separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of mdm10 |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2016-10-01 |
| description |
The protein Mdm10 is known to be present in the endoplasmic reticulum-mitochondria encounter structure (ERMES) and in mitochondrial sorting and assembly machinery (SAM). Here, the authors examine how this protein interacts with SAM and EMRES, showing that the SAM-mediated protein machinery is independent of ERMES. |
| url |
https://doi.org/10.1038/ncomms13021 |
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