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The interactome of human MIC13, a subunit of MICOS complex

ABSTRACT: Description: MIC13 is a subunit of the mitochondrial contact site and cristae organizing system (MICOS) and essential for mitochondrial cristae structure. Here we enriched Mic13 by co-Immunoprecipitation and identified interacting proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Ilka Wittig

LAB HEAD: Ruchika Anand

PROVIDER: PXD044968 | Pride | 2025-01-02

REPOSITORIES: Pride

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			Action	DRS
	P17_089_QIL_IP_KO_01.raw	Raw
	P17_089_QIL_IP_KO_02.raw	Raw
	P17_089_QIL_IP_KO_03.raw	Raw
	P17_089_QIL_IP_KO_04.raw	Raw
	P17_089_QIL_IP_KO_05.raw	Raw

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Publications

SLP2 and MIC13 synergistically coordinate MICOS assembly and crista junction formation.

Naha Ritam R Strohm Rebecca R Schaumkessel Yulia Y Urbach Jennifer J Wittig Ilka I Reichert Andreas S AS Kondadi Arun Kumar AK Anand Ruchika R

iScience 20241123 12

The MICOS complex, essential for cristae organization, comprises MIC10 and MIC60 subcomplexes, with MIC13 as a crucial subunit. <i>MIC13</i> mutations cause severe mitochondrial hepato-encephalopathy, cristae defects, and MIC10-subcomplex loss. We demonstrate that depletion of the mitochondrial protease YME1L in <i>MIC13</i> KO stabilizes MIC10-subcomplex, restoring MIC60-MIC10 interaction and crista junction (CJ) defects, indicating MIC13 is crucial for MIC10-subcomplex stabilization rather tha ...[more]

PMID: 39720525

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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

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

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

Glucose-regulated and drug perturbed beta-cell phosphoproteome reveals molecular mechanisms controlling insulin secretion

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2016-12-09 | PXD003850 | Pride

Quantification of oxidized proteins in wild type and Nox2 deficient mouse dorsal root ganglia

Project description:Here we studied the NOX2 dependent redox-proteome in dorsal root ganglia in mice. The overall goal was to assess the degree of NOX2-dependent changes in oxidised proteins following exposure to enriched enviroment and sciatic nerve axotomy in dorsal root ganglia.

2020-10-13 | PXD018085 | Pride

Endothelial protein interaction partners of the lncRNA PCAT19

Project description:PCAT19 is an endothelial-enriched lncRNA that contributes to the proliferation-quiescence switch in a cell density-dependent manner. Here we performed an antisense-oligonucleotide pulldown of the PCAT19 lncRNA followed by mass spectrometry to identify protein interaction partners of PCAT19. Interaction partners were further analysed for their potential role with PCAT19.

2022-09-29 | PXD032669 | Pride

Protein expression and oxidation in the hippocampus of neuronal nucleoredoxin knockout (Nestin-NXN-/-) versus floxed control mice (NXN-flfl)

Project description:Nucleoredoxin (NXN) is a thioredoxin-like member of the large group of redoxins which maintain redox balances in the cell. Its primary localization is the cytoplasm, and it is highly expressed in neurons. It has been described as a redox regulator of WNT signaling via maintenance of the redox balance of Disheveled (Dvl). Previous proteomic analyses in NXN-knockdown SH-SY5Y cells found a high fraction of reduced proteins involved in development and cell differentiation. The results suggested NXN mainly acted as oxidase under the culture conditions. The functions in vivo are not known, but full deletion of NXN is embryonically lethal owing to cranial deformities. We have generated mice with a pan-neuronal Nestin-Cre driven deletion of NXN (Nestin-NXN-/-) to study its functions in neurons. Nestin-NXN-/- develop normally and are healthy up to old age. They show a loss of exploratory and playful behavior but have no deficits of cognitive functions, social behavior or readouts of anxiety. Using a Yeast-2-Hybrid screen, calcium calmodulin kinase 2a was identified as interaction partner. Camk2a is crucial for long-term potentiation and thereby learning and memory but is also associated with psychiatric diseases, and it is regulated via redox modification of cysteines that impact on the autophosphorylation status of a critical threonine. Camk2a colocalized and co-precipitated with NXN and its activity depended on the presence of NXN. To further study the functions of NXN in neurons we performed a proteomic screen of the hippocampal proteome and the redox proteome using the BIAM switch method.

2021-09-10 | PXD024624 | Pride

Identification of protein interaction partners of the lncRNA ADPGK-AS1

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Antisense affinity selection of the lncRNA NTRAS in HeLa lysate

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2022-04-25 | PXD030620 | Pride

Identification of lncRNA CALA-dependent protein interaction partners of G3BP1 in the cytoplasm

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