Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has...

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Autores principales: Morgenstern, Marcel, Stiller, Sebastian B., Lübbert, Philipp, Peikert, Christian D., Dannenmaier, Stefan, Drepper, Friedel, Weill, Uri, Höß, Philipp, Feuerstein, Reinhild, Gebert, Michael, Bohnert, Maria, van der Laan, Martin, Schuldiner, Maya, Schütze, Conny, Oeljeklaus, Silke, Pfanner, Nikolaus, Wiedemann, Nils, Warscheid, Bettina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5494306/
https://www.ncbi.nlm.nih.gov/pubmed/28658629
http://dx.doi.org/10.1016/j.celrep.2017.06.014
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author Morgenstern, Marcel
Stiller, Sebastian B.
Lübbert, Philipp
Peikert, Christian D.
Dannenmaier, Stefan
Drepper, Friedel
Weill, Uri
Höß, Philipp
Feuerstein, Reinhild
Gebert, Michael
Bohnert, Maria
van der Laan, Martin
Schuldiner, Maya
Schütze, Conny
Oeljeklaus, Silke
Pfanner, Nikolaus
Wiedemann, Nils
Warscheid, Bettina
author_facet Morgenstern, Marcel
Stiller, Sebastian B.
Lübbert, Philipp
Peikert, Christian D.
Dannenmaier, Stefan
Drepper, Friedel
Weill, Uri
Höß, Philipp
Feuerstein, Reinhild
Gebert, Michael
Bohnert, Maria
van der Laan, Martin
Schuldiner, Maya
Schütze, Conny
Oeljeklaus, Silke
Pfanner, Nikolaus
Wiedemann, Nils
Warscheid, Bettina
author_sort Morgenstern, Marcel
collection PubMed
description Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has not been achieved. We developed an integrative experimental approach to define the proteome of east mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions and defined 901 high-confidence mitochondrial proteins, expanding the set of mitochondrial proteins by 82. Our analysis includes protein abundance under fermentable and nonfermentable growth, submitochondrial localization, single-protein experiments, and subcellular classification of mitochondria-associated fractions. We identified mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS), and the coenzyme Q biosynthesis cluster, as well as mitochondrial proteins with dual cellular localization. The integrative proteome provides a high-confidence source for the characterization of physiological and pathophysiological functions of mitochondria and their integration into the cellular environment.
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spelling pubmed-54943062017-07-13 Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale Morgenstern, Marcel Stiller, Sebastian B. Lübbert, Philipp Peikert, Christian D. Dannenmaier, Stefan Drepper, Friedel Weill, Uri Höß, Philipp Feuerstein, Reinhild Gebert, Michael Bohnert, Maria van der Laan, Martin Schuldiner, Maya Schütze, Conny Oeljeklaus, Silke Pfanner, Nikolaus Wiedemann, Nils Warscheid, Bettina Cell Rep Resource Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has not been achieved. We developed an integrative experimental approach to define the proteome of east mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions and defined 901 high-confidence mitochondrial proteins, expanding the set of mitochondrial proteins by 82. Our analysis includes protein abundance under fermentable and nonfermentable growth, submitochondrial localization, single-protein experiments, and subcellular classification of mitochondria-associated fractions. We identified mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS), and the coenzyme Q biosynthesis cluster, as well as mitochondrial proteins with dual cellular localization. The integrative proteome provides a high-confidence source for the characterization of physiological and pathophysiological functions of mitochondria and their integration into the cellular environment. Cell Press 2017-06-27 /pmc/articles/PMC5494306/ /pubmed/28658629 http://dx.doi.org/10.1016/j.celrep.2017.06.014 Text en © 2017 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Resource
Morgenstern, Marcel
Stiller, Sebastian B.
Lübbert, Philipp
Peikert, Christian D.
Dannenmaier, Stefan
Drepper, Friedel
Weill, Uri
Höß, Philipp
Feuerstein, Reinhild
Gebert, Michael
Bohnert, Maria
van der Laan, Martin
Schuldiner, Maya
Schütze, Conny
Oeljeklaus, Silke
Pfanner, Nikolaus
Wiedemann, Nils
Warscheid, Bettina
Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title_full Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title_fullStr Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title_full_unstemmed Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title_short Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale
title_sort definition of a high-confidence mitochondrial proteome at quantitative scale
topic Resource
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5494306/
https://www.ncbi.nlm.nih.gov/pubmed/28658629
http://dx.doi.org/10.1016/j.celrep.2017.06.014
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