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“Identifying the SLC25A46 interactome in transgenic mice: cerebrum”

ABSTRACT: SLC25A46 is an outer mitochondrial protein, member of the mitochondrial carrier family (SLC25), whereas mutations result in mitochondrial structure abnormalities leading to a wide spectrum of neurological disorders. SLC25A46 is known to interact with members of the MICOS (Mitochondrial Contact Site) complex involved in mitochondrial cristae organization, and components of the endoplasmic reticulum membrane. In the present work, our aim was to identify the interactome of SLC25A46 in cerebrum from TgSLC25A46-FLAG transgenic mice through immunoprecipitation with anti-FLAG beads and proteomic analysis with LC-MS/MS.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Telencephalon

SUBMITTER: Martina Samiotaki

LAB HEAD: Eleni Douni

PROVIDER: PXD028421 | Pride | 2022-01-11

REPOSITORIES: Pride

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			Action	DRS
	11925_1.raw	Raw
	11925_2.raw	Raw
	11925_3.raw	Raw
	11926_1.raw	Raw
	11926_2.raw	Raw

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“Identifying the SLC25A46 interactome in transgenic mice: Thymus"

Project description:SLC25A46 is an outer mitochondrial protein, member of the mitochondrial carrier family (SLC25), whereas mutations result in mitochondrial structure abnormalities leading to a wide spectrum of neurological disorders. SLC25A46 is known to interact with members of the MICOS (Mitochondrial Contact Site) complex involved in mitochondrial cristae organization, and components of the endoplasmic reticulum membrane. In the present work, our aim was to identify the interactome of SLC25A46 in cerebrum, cerebellum, heart and thymus from TgSLC25A46-FLAG transgenic mice through immunoprecipitation with anti-FLAG beads and proteomic analysis with LC-MS/MS.

2022-01-11 | PXD027603 | Pride

“Identifying the SLC25A46 interactome in transgenic mice: cerebellum”

2022-01-11 | PXD027599 | Pride

“Identifying the SLC25A46 interactome in transgenic mice: Heart"

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Mitochondrial cristae architecture protects against mtDNA release and inflammation

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Diverged Trypanosome MICOS as a Hub for Mitochondrial Cristae Shaping and Protein Import

Project description:The mitochondrial contact site and cristae organization system (MICOS) is a complex responsible for proper cristae formation. Empirical data about this ubiquitous complex is limited to opisthokont models (e.g. yeast), impeding understanding of its core properties and adaptation potential to diverse cellular milieus. To close this knowledge gap, we characterized MICOS from the diverged excavate Trypanosoma brucei. These results allow the definition of fundamental MICOS properties, such as its role in maintaining both cristae and contacts between the inner and outer membranes plus its extrusion into the intermembrane space. Yet, surprising differences with opisthokonts indicate that MICOS can assume different forms. T. brucei MICOS contains a novel subunit involved in the import of intermembrane space proteins, including respiratory chain complex assembly factors. We propose an evidence-based hypothesis that T. brucei MICOS populates cristae membranes with proteins needed for respiration, supported by the complex's even distribution in cristae

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MICOS and F1FO-ATP synthase crosstalk is a fundamental property of mitochondrial cristae

Project description:Mitochondrial cristae are polymorphic invaginations of the inner membrane that are the fabric of cellular respiration. Both the Mitochondrial Contact Site and Cristae Organization System (MICOS) and the F1FO-ATP synthase are vital for sculpting cristae by opposing membrane bending forces. While MICOS promotes negative curvature at cristae junctions, dimeric F1FO-ATP synthase is crucial for positive curvature at cristae rims. Crosstalk between these two complexes has been observed in baker’s yeast, the model organism of the Opisthokonta supergroup. Here, we report that this property is conserved in Trypanosoma brucei, a member of the Discoba supergroup that separated from Opisthokonta ~2 billion years ago. Specifically, one of the paralogs of the core MICOS subunit Mic10 interacts with dimeric F1FO-ATP synthase, whereas the other core Mic60 subunit has a counteractive effect on F1FO-ATP synthase oligomerization. This is evocative of the nature of MICOS-F1FO-ATP synthase crosstalk in yeast, which is remarkable given the diversification these two complexes have undergone during almost 2 eons of independent evolution. Furthermore, we identified a highly diverged trypanosome homolog of subunit e, which is essential for the stability of F1FO-ATP synthase dimers in yeast. Just like subunit e, it is preferentially associated with dimers, interacts with Mic10 and its silencing results in severe defects to cristae and disintegration of F1FO-ATP synthase dimers. Our findings indicate that crosstalk between MICOS and dimeric F1FO-ATP synthase is a fundamental property impacting cristae shape throughout eukaryotes.

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Integrative Genomics Positions MKRN1 as a Novel Ribonucleoprotein within the Embryonic Stem Cell Gene Regulatory Network

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RCCD1 also Resides in Mitochondria to Regulate mtDNA Dynamics and Mitochondrial Homeostasis

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