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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: Heart"

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 | PXD027622 | Pride

“Identifying the SLC25A46 interactome in transgenic mice: Thymus"

2022-01-11 | PXD027603 | Pride

“Identifying the SLC25A46 interactome in transgenic mice: cerebellum”

2022-01-11 | PXD027599 | Pride

Mitochondrial cristae architecture protects against mtDNA release and inflammation

Project description:Mitochondrial damage causes mtDNA release to activate type I interferon (IFN-I) response via the cGAS-STING pathway. mtDNA-induced inflammation promotes autoimmune and aging-related degenerative disorders. However, the global picture of inflammation-inducing mitochondrial damages remains obscure. Here we performed a mitochondria-targeted CRISPR-knockout screen for regulators of the IFN-I response. Strikingly, our screen revealed dozens of hits enriched with key regulators of cristae architecture, including phospholipid cardiolipin and protein complexes such as OPA1, MICOS, SAM, MIB, PHB, and the F1Fo-ATP synthase. Disrupting these cristae organizers consistently induced mtDNA release and STING-dependent IFN-I response. Furthermore, robust STING-dependent IFN-I response was induced in vivo by knocking out MTX2, a subunit of the SAM complex whose null-mutations cause progeria in human. Taken together, beyond revealing the central role of cristae architecture to prevent mtDNA release and inflammation, our results mechanistically link mitochondrial cristae disorganization and inflammation, two emerging hallmarks of aging and aging-related degenerative diseases.

2022-10-28 | GSE216499 | GEO

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

2018-09-13 | PXD009601 | Pride

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.

2021-06-15 | PXD025109 | Pride

Complexome profiling of MICOS complex, impact of subunits MIC26 and MIC27

Project description:Here we analysed the impact of two subunits (MIC26 and MIC27) on the assembly and stability of the mitochondrial contact site and cristae organizing system (MICOS) complex.

2020-07-28 | PXD016732 | Pride

Complexome profiling of mitochondrial protein complexes in single and double MIC26 and MIC27 knockout cells

Project description:Here we analysed the impact of two subunits of the mitochondrial contact site and cristae organizing system (MICOS) complex, MIC26 and MIC27, on the assembly and stability of mitochondrial complexes of the oxidative phosphorylation system (OXPHOS).

2020-07-28 | PXD016733 | Pride

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

Project description:For identification of proteins that associate with Makorin1 (MKRN1) in RNA-dependent and RNA-independent manners, we affinity purified FLAG-tagged Makorin1 (MKRN1) from mouse embryonic stem cells constitutively expressing FLAG:MKRN1. Anti-FLAG control immunoprecipitations were performed from a FLAG vectrol control (FLAG:Ctrl) mouse embryonic stem cell line that did not express FLAG:MKRN1. Following FLAG immunoprecipitation, anti-FLAG beads from FLAG:MKRN1 and FLAG:Ctrl immunoprecipitations were split into separate tubes such that half of the beads were digested with 200Ã∞â≈ Ã≠Âµg/mL RNase A while the other half of the beads were undigested. RNase A-digested and undigested immunoprecipitates were subjected to LC-MS/MS analysis. Of the 48 RNA-related proteins previously identified to associate with FLAG:MKRN1, L1TD1, PABPC1, PABPC4, YBX1, IGF2BP1 and UPF1 were found to remain associated with FLAG:MKRN1 in the presence of RNase A.

2015-07-21 | PXD001291 | Pride

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

Project description:Regulator of chromosome condensation domain-containing protein 1 (RCCD1) plays an important role in chromosome segregation and microtubule stability in the nucleus and has been identified recently as a potential driver for breast cancer. We report here that, unexpectedly, RCCD1 is also localized in mitochondria. We show that RCCD1 resides in the mitochondrial inner membrane, where it interacts with the mitochondrial contact site/cristae organizing system (MICOS) and mitochondrial DNA (mtDNA) to regulate mitochondrial nucleoid organization, thereby influencing mtDNA transcription, oxidative phosphorylation, and the production of reactive oxygen species. Interestingly, RCCD1 is upregulated under hypoxic conditions, leading to decreased generation of reactive oxygen species and alleviated apoptosis favoring cancer cell survival. We show that RCCD1 promotes breast cancer cell proliferation in vitro and accelerates breast tumor growth in vivo. Indeed, RCCD1 is overexpressed in breast carcinomas, and its level of expression is associated with aggressive breast cancer phenotypes and poor patient survival. Our study reveals an additional dimension in RCCD1 functionality, indicating RCCD1 is an essential regulator of mtDNA dynamics and mitochondrial homeostasis, whose dysregulation inflicts pathologic states such as breast cancer.

2023-12-01 | GSE219134 | GEO

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