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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9bf2b01669244292939e16b34fde2489
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spelling	oai:doaj.org-article:9bf2b01669244292939e16b34fde24892021-12-02T17:32:35ZSeparating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm1010.1038/ncomms130212041-1723https://doaj.org/article/9bf2b01669244292939e16b34fde24892016-10-01T00:00:00Zhttps://doi.org/10.1038/ncomms13021https://doaj.org/toc/2041-1723The 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.Lars EllenriederŁukasz OpalińskiLars BeckerVivien KrügerOliver MirusSebastian P. StraubKatharina EbellNadine FlinnerSebastian B. StillerBernard GuiardChris MeisingerNils WiedemannEnrico SchleiffRichard WagnerNikolaus PfannerThomas BeckerNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2016
url	https://doaj.org/article/9bf2b01669244292939e16b34fde2489
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Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

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