| Literature DB >> 34800366 |
Marcel Morgenstern1, Christian D Peikert1, Philipp Lübbert2, Ida Suppanz1, Cinzia Klemm1, Oliver Alka1, Conny Steiert3, Nataliia Naumenko4, Alexander Schendzielorz1, Laura Melchionda5, Wignand W D Mühlhäuser1, Bettina Knapp1, Jakob D Busch3, Sebastian B Stiller3, Stefan Dannenmaier1, Caroline Lindau3, Mariya Licheva2, Christopher Eickhorst6, Riccardo Galbusera7, Ralf M Zerbes3, Michael T Ryan8, Claudine Kraft5, Vera Kozjak-Pavlovic9, Friedel Drepper1, Sven Dennerlein4, Silke Oeljeklaus1, Nikolaus Pfanner10, Nils Wiedemann11, Bettina Warscheid12.
Abstract
Mitochondria are key organelles for cellular energetics, metabolism, signaling, and quality control and have been linked to various diseases. Different views exist on the composition of the human mitochondrial proteome. We classified >8,000 proteins in mitochondrial preparations of human cells and defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP). We identified interactors of translocases, respiratory chain, and ATP synthase assembly factors. The abundance of MitoCoP proteins covers six orders of magnitude and amounts to 7% of the cellular proteome with the chaperones HSP60-HSP10 being the most abundant mitochondrial proteins. MitoCoP dynamics spans three orders of magnitudes, with half-lives from hours to months, and suggests a rapid regulation of biosynthesis and assembly processes. 460 MitoCoP genes are linked to human diseases with a strong prevalence for the central nervous system and metabolism. MitoCoP will provide a high-confidence resource for placing dynamics, functions, and dysfunctions of mitochondria into the cellular context.Entities:
Keywords: Mitochondria; complexome; copy numbers; disease; half-lives; high-confidence proteome; human cells; protein translocation; respiratory chain; smORFs
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Year: 2021 PMID： 34800366 PMCID： PMC8664129 DOI： 10.1016/j.cmet.2021.11.001
Source DB: PubMed Journal: Cell Metab ISSN： 1550-4131 Impact factor: 27.287