Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

Ellenrieder, Lars; Opaliński, Łukasz; Becker, Lars; Krüger, Vivien; Mirus, Oliver; Straub, Sebastian; Ebell, Katharina; Flinner, Nadine; Stiller, Sebastian B.; Guiard, Bernard; Meisinger, Chris; Wiedemann, Nils; Schleiff, Enrico; Wagner, Richard; Pfanner, Nikolaus; Becker, Thomas

doi:10.1038/ncomms13021

Cited by 73 publications

(102 citation statements)

References 63 publications

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“…The ER-mitochondria encounter structure (ERMES) revealed a remarkable separation with three subunits present in class 1 and two in class 3. This dual distribution is consistent with data from previous work showing that Mdm10, Mdm34, and Gem1 are anchored in the mitochondrial outer membrane, whereas Mmm1 localizes to the ER membrane and Mdm12 is bridging Mmm1 and Mdm34/Mdm10 at the cytosolic side (Ellenrieder et al., 2016, Kornmann et al., 2009). Various proteins controlling mitochondrial fusion and fission were also present in class 1, albeit with a broader distribution (Figure 2F).…”

Section: Resultssupporting

confidence: 92%

Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

et al. 2017

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SummaryMitochondria 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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Section: Resultssupporting

confidence: 92%

Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

et al. 2017

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“…Interestingly, several mitochondrial tethers bind proteins that have a role in translocation and this might serve as a way to regulate these functions. One of the most studied examples is the shuttling of Mdm10 between the ERMES complex, where it functions in tethering, and the SAM complex, where it promotes the biogenesis of α-helical and β-barrel proteins [8]. Lam6 also interacts with Tom70/71 and EMCs interact with Tom5 [10,13,14].…”

Section: Discussionmentioning

confidence: 99%

Mitochatting – If only we could be a fly on the cell wall

Eisenberg-Bord

Schuldiner

2017

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Mitochondria, cellular metabolic hubs, perform many essential processes and are required for the production of metabolites such as ATP, iron-sulfur clusters, heme, amino acids and nucleotides. To fulfill their multiple roles, mitochondria must communicate with all other organelles to exchange small molecules, ions and lipids. Since mitochondria are largely excluded from vesicular trafficking routes, they heavily rely on membrane contact sites. Contact sites are areas of close proximity between organelles that allow efficient transfer of molecules, saving the need for slow and untargeted diffusion through the cytosol. More globally, multiple metabolic pathways require coordination between mitochondria and additional organelles and mitochondrial activity affects all other cellular entities and vice versa. Therefore, uncovering the different means of mitochondrial communication will allow us a better understanding of mitochondria and may illuminate disease processes that occur in the absence of proper cross-talk. In this review we focus on how mitochondria interact with all other organelles and emphasize how this communication is essential for mitochondrial and cellular homeostasis. This article is part of a Special Issue entitled: Membrane Contact Sites edited by Christian Ungermann and Benoit Kornmann.

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“…On the one side it associates with the SAM complex to promote the assembly of the TOM complex. On the other side it forms the mitochondrial membrane anchor of the ER‐mitochondria encounter structure (ERMES) . The ERMES complex forms a molecular tether between the ER and mitochondria that is crucial to maintain mitochondrial morphology and lipid homeostasis .…”

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

“…Thus, coupling to different partner proteins allows Mdm10 to carry out distinct functions for mitochondrial biogenesis. Upon reconstitution into a lipid bilayer recombinant Mdm10 forms a slight cation‐selective channel with a maximal conductance of 480 pS . In this context, it is particularly interesting, that addition of Tom22 specifically induces fast gating of the Mdm10 channel pore.…”

Section: Channel‐forming Proteins In Protein Transportmentioning

confidence: 99%

“…Two new channels involved in protein transport have been identified. The mitochondrial division and morphology protein 10 (Mdm10) forms a β‐barrel channel that mediates the biogenesis of the TOM complex . Mim1 of the mitochondrial import machinery (MIM) promotes biogenesis of α‐helical outer membrane proteins and constitutes the first outer membrane channel with a predicted α‐helical structure .…”

Section: Introductionmentioning

confidence: 99%

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Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker

Wagner

2018

BioEssays

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Mitochondrial function and biogenesis depend on the transport of a large variety of proteins, ions, and metabolites across the two surrounding membranes. While several specific transporters are present in the inner membrane, transport processes across the outer membrane are less understood. Recent studies reveal that the number of outer membrane channels and their transport mechanisms are more diverse than originally thought. Four protein-conducting channels promote transport of distinct sets of precursor proteins across and into the outer membrane. The voltage-dependent anion channel (VDAC) forms the major channel for small hydrophilic molecules. In addition, three channels with yet unknown substrate specificity exist in the outer membrane. In this review, we outline the emerging functional diversity, selectivity, and regulation of mitochondrial outer membrane channels. The presence of several channel-forming proteins challenges the traditional view that the outer membrane forms an unspecific size-exclusion filter for the flux of small hydrophilic molecules.

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Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

Cited by 73 publications

References 63 publications

Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale

Mitochatting – If only we could be a fly on the cell wall

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

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