Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mitochondrial translocase TOMM22 is overexpressed in pancreatic cancer and promotes aggressive growth by modulating mitochondrial protein import and function

ABSTRACT: Dysregulated mitochondrial function is a common feature in several malignancies, includingpancreatic cancer. Although mitochondria have their own genome, most mitochondrial proteins are nuclear-encoded and imported by a multi-subunit translocase of the outer mitochondrial membrane (TOMM). TOMM22 is the central receptor of the TOMM complex and plays a role incomplex assembly. We aim to understand the pathobiological roles of TOMM subunits in PC.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Pancreas

DISEASE(S): Pancreatic Cancer

SUBMITTER: SANTANU DASGUPTA

LAB HEAD: Santanu Dasgupta

PROVIDER: PXD040198 | Pride | 2023-10-25

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Analysis of mitochondrial gene expression with Ribosome Profiling

Project description:Ribosome profiling (RiboSeq) maps positions of translating ribosomes on the transcriptome. Here we optimized ribosome profiling for footprinting mitochondrial ribosomes, and profiled three human cell-lines - HEK293, a PDE12-/- knockout, and a deltaFLP 143B cybrid.

2017-07-25 | E-MTAB-5519 | biostudies-arrayexpress

Phosphorylation of claudin-11 - Mass spectrometry analysis confirmed the phosphorylation of human claudin-11 at tyrosine 191 and tyrosine 192

Project description:Mass spectrometry analysis confirmed the phosphorylation of human claudin-11 at tyrosine 191 and tyrosine 192

2018-08-29 | PXD010908 | Pride

The human mitochondrial transcriptome

Project description:The human mitochondrial genome comprises a distinct genetic system transcribed as precursor polycistronic transcripts that are subsequently cleaved to generate individual mRNAs, tRNAs and rRNAs. Here we provide a comprehensive analysis of the human mitochondrial transcriptome across multiple cell lines and tissues. Using directional deep sequencing and parallel analysis of RNA ends, we demonstrate wide variation in mitochondrial transcript abundance, and precisely resolve transcript processing and maturation events. We identify novel transcripts, including small RNAs, and observe the enrichment of several nuclear RNAs in mitochondria. Using high-throughput in vivo DNaseI footprinting, we establish the global profile of DNA-binding protein occupancy across the mitochondrial genome at single nucleotide resolution, revealing novel regulatory features at mitochondrial transcription initiation sites and functional insights into disease-associated variants. Together, this integrated analysis of the mitochondrial transcriptome reveals unexpected complexity in the regulation, expression, and processing of mitochondrial RNA, and itM-CM-^BM-BM- provides a resource for the future study of mitochondrial function (accessed at mitochondria.matticklab.com). Examination of the mitochondiral transcriptome by long and small RNA sequencing, PARE sequencing and DNAseI hypersensitivity mapping.

2011-07-20 | E-GEOD-30772 | biostudies-arrayexpress

Peroxisomal targeting of the protein phosphatase Ptc5 via mitochondrial transit

Project description:Correct intracellular distribution of proteins is critical for the function of eukaryotic cells. Certain proteins are targeted to more than one cellular compartment, e.g. to mitochondria and peroxisomes. The protein phosphatase Ptc5 from Saccharomyces cerevisiae contains an N-terminal mitochondrial presequence followed by a trans-membrane domain and has been detected in the mitochondrial intermembrane space. Here we show mitochondrial transit of Ptc5 to peroxisomes. Translocation of Ptc5 to peroxisomes depended both on the C-terminal peroxisomal targeting signal (PTS1) and N-terminal cleavage by the mitochondrial inner membrane peptidase complex. Indirect targeting of Ptc5 to peroxisomes prevented deleterious effects of its phosphatase activity in the cytosol. Sorting of Ptc5 involves simultaneous interaction with import machineries of both organelles. We identify additional mitochondrial proteins with PTS1, which localize in both organelles and can increase their physical association. Thus, a tug-of-war like mechanism can influence the interaction and communication of two cellular compartments.

2020-05-22 | PXD018591 | Pride

Oxidative burden and mitochondrial dysfunction in a mouse model of Rett syndrome

Project description:To identify the detailed molecular causes of the mitochondrial dysfunction, oxidative burden and more vulnerable redox balance in Rett mouse hippocampus, we screened for differential gene expression in the hippocampal CA1 subfield of adult male mice. A whole mouse genome microarray was performed to assess, whether key enzymes of the mitochondrial respiratory chain or major cellular radical scavenging enzymes are affected in this MeCP2-deficient mouse model of Rett syndrome. Comparison of gene expression between male wildtype mice (Mecp2+/y) and mice lacking the MECP2 gene (Mecp2-/y) [B6.129P2(C)-Mecp2tm-1-1Bird (Guy et al. 2001, Nat. Genet. 27: 322-326)]. In total, 9 mice of each genotype were analyzed. The mRNA of groups of 3 animals was pooled to generate 3 independent biological samples, and finally three microarrays were run for each genotype.

2012-08-31 | E-GEOD-32870 | biostudies-arrayexpress

DNA-seq of mitochondrial DNA from mouse heart that is both heart SOD2 knockout and deficient for mitochondrial DNA repair

Project description:To study whether increase in mitochondrial oxidative stress (SOD2 removal) and decrease in mitochondrial DNA repair (Ogg1 dMTS) results into increase in mitochondrial DNA mutation load. Oxidative stress has been suggested to induce mutations in mtDNA. To verify this, we extracted and sequenced (Illumina) mitochondrial DNA from heart Sod2 knockout animals that were also deficient for mitochondrial base-excision repair. The repair deficiency was induced by removing the genomic region encoding for the predicted mitochondrial targeting sequence from endogenous OGG1 (L2 to W23) called Ogg1 dMTS mice, thus excluding the protein from mitochondria. OGG1 is a DNA glycosylase that recognizes and repairs 8-oxo-dG damage from DNA. Oxidative stress can induce 8-oxo-dG lesions, thus we removed the mitochondrial matrix localized superoxide dismutase (SOD2) from these mice to increase the level of oxidative stress. 8-oxo-dG lesion can be mutagenic because some DNA repair polymerases are known to erroneously incorporate adenosine opposite to 8-oxo-dG during replication leading to GC>TA transversion mutations.

2018-07-13 | E-MTAB-6533 | biostudies-arrayexpress

Establishment of functional protein interaction networks of so far undescribed human mitochondrial proteins by q-AP-MS

Project description:The overall aim of the project is the definition and characterization of the mitochondrial proteome of human cells, referred to as MitoCoP. To this end, we combined complementary strengths of subtractive proteomics, ImportOmics and subcellular protein profiling in a global multidimensional classification approach (see dataset 'Definition and characterization of the mitochondrial proteome of human cells (MitoCoP)'). SILAC-based affinity purification-mass spectrometry (q-AP-MS) experiments were performed to establish functional protein interaction networks of so far undescribed mitochondrial proteins.

2021-11-25 | PXD018182 | Pride

Crosstalk between Drp1 phosphorylations during mitochondrial remodelling and their impact on metabolic adaptation - Parallel reaction monitoring (PRM) mass spectrometry-based proteomic data

Project description:Mitochondria constantly undergo fusion and fission events, referred as mitochondrial dynamics, which determine intracellular mitochondrial architecture and bioenergetics. Cultured cell studies demonstrate that mitochondrial dynamics are acutely regulated by phosphorylation of the mitochondrial fission orchestrator Drp1, at S579 or S600. This dataset is linked to a study reporting on how in differentiated mouse tissues Drp1 phosphorylation at S600 acted as an upstream event for S579 phosphorylation, leading to mitochondrial fragmentation. We performed liquid chromatography mass spectrometry (LC-MS) analyses in phospho-Drp1 immunoprecipitates from BAT of vehicle or CL316,243-treated mice, following digestion with endoproteinase Glu-C to assess whether S600 and S579 phosphorylations were both occurring in the same Drp1 proteoforms or individually in different pools of Drp1 proteins. Our results certify that upon PKA stimulation, S600 and S579 phosphorylations occurred simultaneously on the same Drp1 molecular form.

2021-08-26 | PXD027108 | Pride

Expression data from rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct

Project description:RNF10 is a synapse-to-nucleus protein messsenger regulating NMDAR-dependent gene trascription. We have charaterized the impact of the absence of RNF10 on structural synaptic plasticity. In this dataset we included expression data from homogenates of DIV14 rat organotypic hippocampal slices lentivirally infected with shRNF10 or scramble construct 8 total samples were analyzed (4 shRNF10 and 4 scramble).

2015-06-20 | E-GEOD-69267 | biostudies-arrayexpress

Sexual dimorphism in the zebrafish eye proteins

Project description:The present study aims to apply a high-resolution and label-free proteomics approach to identify and quantify proteins in the eye of zebrafish. First, the results of the present study will provide a comprehensive list of proteins in the eye of zebrafish, and second, establish a platform based on sex-biased proteins that may offer clues to answer crucial questions such as sex-based differences in visual perception and impairments. Our results may improve the outcome of behavioural, developmental, toxicological, and medical experiments considering the zebrafish eye.

2024-03-04 | PXD033338 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data