Tom7 Regulates Mdm10-mediated Assembly of the Mitochondrial Import Channel Protein Tom40

Yamano, Koji; Tanaka‐Yamano, Sachiko; Endo, Toshiya

doi:10.1074/jbc.m110.163238

Cited by 87 publications

(87 citation statements)

References 32 publications

(45 reference statements)

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“…These results substantiate our aforementioned findings that Mcp1 and Mcp2 have no direct function in the assembly of the TOM complex. It is well documented that alterations in Mdm10 levels affect the amounts of various forms of the TOB complex (Thornton et al, 2010;Yamano et al, 2010b;Yamano et al, 2010a;Becker et al, 2011). In agreement with these reports, we observed three different TOB-complex species (Fig.…”

Section: Mcp1 and Mcp2 Are High-copy Suppressors Of Mdm10dsupporting

confidence: 82%

Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis

Tan

Özbalci

Brügger

et al. 2013

Journal of Cell Science

120

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SummaryThe yeast mitochondrial outer membrane (MOM) protein Mdm10 is involved in at least three different processes: (1) association of mitochondria with the endoplasmic reticulum and mitochondrial lipid homeostasis (2) membrane assembly of MOM proteins, and (3) inheritance and morphogenesis of mitochondria. To decipher the precise role of Mdm10 in mitochondrial function, we screened for high-copy suppressors of the severe growth defect of the mdm10D mutant. We identified two novel mitochondrial proteins (open reading frames YOR228c and YLR253w) that we named Mdm10 complementing protein (Mcp) 1 and Mcp2. Overexpression of Mcp1 or Mcp2 restores the alterations in morphology and stability of respiratory chain complexes of mitochondria devoid of Mdm10, but the observed defect in assembly of MOM proteins is not rescued. Lipid analysis demonstrates that elevated levels of Mcp1 and Mcp2 restore the alterations in mitochondrial phospholipid and ergosterol homeostasis in cells lacking Mdm10. Collectively, this work identifies two novel proteins that play a role in mitochondrial lipid homeostasis and describes a role of Mdm10 in ergosterol trafficking.

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Section: Mcp1 and Mcp2 Are High-copy Suppressors Of Mdm10dsupporting

confidence: 82%

Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis

Tan

Özbalci

Brügger

et al. 2013

Journal of Cell Science

120

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“…In yeast, Tom7 is a non-essential protein that negatively regulates TOM complex assembly (48,49). Loss of Tom7 in yeast therefore promotes TOM complex assembly.…”

Section: Discussionmentioning

confidence: 99%

The Import of Proteins into the Mitochondrion of Toxoplasma gondii

Dooren

Yeoh

Striepen

et al. 2016

Journal of Biological Chemistry

146

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Outside of well characterized model eukaryotes, relatively little is known about the translocons that transport proteins across the two membranes that surround the mitochondrion. Apicomplexans are a phylum of intracellular parasites that cause major diseases in humans and animals and are evolutionarily distant from model eukaryotes such as yeast. Apicomplexans harbor a mitochondrion that is essential for parasite survival and is a validated drug target. Here, we demonstrate that the apicomplexan Toxoplasma gondii harbors homologues of proteins from all the major mitochondrial protein translocons present in yeast, suggesting these arose early in eukaryotic evolution. We demonstrate that a T. gondii homologue of Tom22 (TgTom22), a central component of the translocon of the outer mitochondrial membrane (TOM) complex, is essential for parasite survival, mitochondrial protein import, and assembly of the TOM complex. We also identify and characterize a T. gondii homologue of Tom7 (TgTom7) that is important for parasite survival and mitochondrial protein import. Contrary to the role of Tom7 in yeast, TgTom7 is important for TOM complex stability, suggesting the role of this protein has diverged during eukaryotic evolution. Together, our study identifies conserved and modified features of mitochondrial protein import in apicomplexan parasites.

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“…It seems likely that the dually localized Mdm10 protein links the different roles of ERMES. Interestingly, the small TOM protein Tom7 was shown to regulate the dynamic interaction of Mdm10 with the SAM and ERMES complexes Yamano et al 2010;Becker et al 2011a).…”

Section: Diverse Pathways For Trafficking To the Mitochondrial Outer mentioning

confidence: 99%

Mechanisms of Protein Sorting in Mitochondria

Stojanovski

Bohnert

Pfanner

et al. 2012

Cold Spring Harbor Perspectives in Biology

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A protein's function is intimately linked to its correct subcellular location, yet the machinery required for protein synthesis is predominately cytosolic. How proteins are trafficked through the confines of the cell and integrated into the appropriate cellular compartments has puzzled and intrigued researchers for decades. Indeed, studies exploring this premise revealed elaborate cellular protein translocation and sorting systems, which ensure that all proteins are shuttled to the appropriate cellular destination, where they fulfill their specific functions. This holds true for mitochondria, where sophisticated molecular machines serve to recognize incoming precursor proteins and integrate them into the functional framework of the organelle. We summarize the recent progress in our understanding of mitochondrial protein sorting and the machineries and mechanisms that mediate and regulate this highly dynamic cellular process essential for survival of virtually all eukaryotic cells.

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Tom7 Regulates Mdm10-mediated Assembly of the Mitochondrial Import Channel Protein Tom40

Cited by 87 publications

References 32 publications

Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis

Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis

The Import of Proteins into the Mitochondrion of Toxoplasma gondii

Mechanisms of Protein Sorting in Mitochondria

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