Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Identification of novel protein binders of human MIRO2 in prostate cancer

ABSTRACT: In previous studies, we showed that MIRO2 mRNA is up-regulated in primary cancer versus normal tissues, across multiple tumor types. MIRO2 had been previously studied in the context of non-tumorigenic cells, where it coordinates microtubule- and actin-based mitochondrial movement. However, we showed that cancer cells utilize MIRO2’s canonical function on mitochondrial trafficking exclusively under conditions of cellular stress that exacerbate mitochondrial dynamics. Thus, identifying MIRO2’s protein binding partners would shed light on the molecular function of MIRO2 in prostate cancer. To this end, we identified the proteins co-precipitating with FLAG-MIRO2 from PC3 cells. Network analysis of MIRO2 binding partners identified metabolism, cell cycle and cellular responses to extracellular stimuli amongst the top over-represented pathways.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Monika Dzieciatkowska

LAB HEAD: Cecilia Caino

PROVIDER: PXD029490 | Pride | 2021-11-25

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20180326_CAINO_01_band01.raw	Raw
	20180326_CAINO_01_band01__F124442_.mzid.gz	Mzid
	20180326_CAINO_01_band01__F124442_.mzid_20180326_CAINO_01_band01__F124442_.MGF	Mzid
	20180326_CAINO_01_band02.mgf	Mgf
	20180326_CAINO_01_band02.raw	Raw

Items per page:

1 - 5 of 96

Similar Datasets

Evaluation of the p53 isoform Δ133p53β aggregation capacity

Project description:p53 isoforms and particularly Δ133p53β play a critical role in cancer progression. We demonstrate that WT Δ133p53β activity is regulated through an aggregation-dependent mechanism. Creation of WT Δ133p53β aggregates depends on associations with specific interacting partners and was observed both in cancer cell lines and in human tumour biopsies.

2021-06-04 | PXD022998 | Pride

Dynamic profiling of the protein life cycle in response to pathogens (protein)

Project description:Protein expression is regulated by production and degradation of mRNAs and proteins, but their specific relationships remain unknown. We combine measurements of protein production and degradation and mRNA dynamics to build a quantitative genomic model of the differential regulation of gene expression in LPS stimulated mouse dendritic cells. Changes in mRNA abundance play a dominant role in determining most dynamic fold changes in protein levels. Conversely, the preexisting proteome of proteins performing basic cellular functions is remodeled primarily through changes in protein production or degradation, accounting for over half of the absolute change in protein molecules in the cell. Thus, the proteome is regulated by transcriptional induction of novel cellular functions and remodeling of preexisting functions through the protein life cycle. Mouse primary dendritic cells were treated with LPS or mock stimulus and profiled over a 12-hour time course. Cells were grown in M-labeled SILAC media, which was replaced with H-labeled SILAC media at time 0. Aliquots were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, 9, and 12 hours post-stimulation and added to equal volumes of a master mix of unlabeled (L) cells for the purpose of normalization. RNA-Seq was performed at 0, 1, 2, 4, 6, 9, and 12 hours post-stimulation.

2015-03-06 | E-GEOD-59792 | biostudies-arrayexpress

Analysing the Mechanism of Mitochondrial Oxidation-induced Cell Death Using a Multifunctional Iridium(III) Photosensitiser

Project description:Mitochondrial oxidation-induced cell death, a physiological process triggered by various cancer therapeutics to induce oxidative stress on tumours, has been challenging to investigate owing to the difficulties in generating mitochondria-specific oxidative stress and monitoring mitochondrial responses simultaneously. Accordingly, to the best of our knowledge, the relationship between mitochondrial protein oxidation via oxidative stress and the subsequent cell death-related biological phenomena has not been defined. Here, we developed a multifunctional iridium(III) photosensitiser, Ir-OA, capable of inducing substantial mitochondrial oxidative stress and monitoring the corresponding change in viscosity, polarity, and morphology. Photoactivation of Ir-OA triggers chemical modifications in mitochondrial protein-crosslinking and oxidation (i.e., Oxidative phosphorylation complexes and channel and translocase proteins), leading to microenvironment changes, such as increased microviscosity and depolarisation. These changes are strongly related to cell death by inducing mitochondrial swelling with excessive fission and fusion. We suggest a potential mechanism from mitochondrial oxidative stress to cell death based on proteomic analyses and phenomenological observations.

2021-03-23 | PXD022163 | Pride

NANOG metabolically reprograms tumor-initiating stem-like cells in oxidative phosphorylation and fatty acid metabolism

Project description:Stem cell markers such as NANOG have been implicated in various cancers; however, the functional contribution of NANOG to cancer pathogenesis has remained unclear. In the present study, we show that Toll-like receptor 4 (TLR4) signaling phosphorylates E2F1 to transactivate NANOG. Down-regulation of Nanog significantly reduces tumor development. In the search for the NANOG-dependent mechanisms underlying growth of tumor-initiating stem-like cells (TICs), NANOG ChIP-seq identifies the genes associated with mitochondrial metabolic pathways. Genome wide Identification of Nanog binding partners in tumor initating stem cells

2016-01-07 | E-GEOD-68237 | biostudies-arrayexpress

Identification of phosphorylation sites on purified recombinant protein Dynamin-like protein 1

Project description:Drp1 is a GTPase involves in mitochondrial division. The phosphorylation of Drp1 is reported to influence Drp1 activity. Two well known Drp1 phosphorylation sites have been identified. In here, we in vitro phosphorylate S579 site by ERK2 kinase on WT-Drp1 or S600D-Drp1 mutant and try to identify the phosphorylation by Mass Spec.

2024-06-16 | PXD046824 | Pride

Lateral interactions between B7-H3 and CD147 are essential for stemness in breast cancer: a novel insight from proximal proteome analysis

Project description:Oncogenic cell-surface membrane proteins contribute to the phenotypic and functional characteristics of cancer stem cells (CSCs). We quantitatively analyzed cell-surface membrane proteins that are in close proximity to CD147 in CSCs using proximity-labeling proteomic approach. Moreover, we compared CSCs to non-CSCs to identify CSC-specific cell-surface membrane proteins that are the nearest neighbors of CD147 and revealed that lateral interaction between CD147 and CD276 (B7H3) concealed within the lipid raft microdomain in CSCs confers resistance to docetaxel, known to treat many types of cancer patients including metastatic breast cancer. Furthermore, we found that co-expression of CD147 and CD276 in patients with HER2+ breast cancer who received chemotherapy had poor disease-free survival (DFS) and Overall survival (OS) rates (p = 0.04 and 0.08, respectively). Subsequent immunohistochemical analysis indicated that co-expression of CD147 and CD276 may be associated with poor response to chemotherapy in an independent HER2+ BC cohort. Altogether, our study suggests that the lateral interaction between CD147 and its proximal partners, such as CD276, may be related to a poor prognostic factor in BC and a predictive marker for the critical phenotypic determinant of breast cancer stemness.

2023-10-24 | PXD036909 | Pride

Mitoribosome profiling (MitoRiboSeq) data from HEK WT and mtRF1 knockout cell lines

Project description:Mitochondrial translation was investigated by mitochondrial ribosome profiling (mitoRiboSeq) in three HEK293 cell lines: HEK293 wildtype, mtRF1 knockout 1, and mtRF1 knockout 2

2022-12-01 | E-MTAB-11687 | biostudies-arrayexpress

Elevated PAF1-RAD52 Axis Confers Chemoresistance to Human Cancers

Project description:To identify a common protein that interacts with PAF1 in ovarian cancer, lung Cancer, and pancreatic cancer to mediate chemoresistance.

2024-01-26 | PXD039281 | Pride

p166 links membrane and intramitochondrial modules of the trypanosomal tripartite attachment complex

Project description:p166 is a central component of a protein complex that is essential for mitochondrial genome segregation in Trypanosoma brucei. The last 34 aa (the C-tail) of p166 are absolutely essential for its function of p166. The prupose of this experiment is to find even putative binding partners interacting with p166. For this purpose, two CoIP experiments with a truncated soluble version of p166 were performed. One uses p166 with an intact C-tail whereas the C-tail is removed in a second experiment. Differences between the two CoIPs indicate potential interactors of the C-tail.

2022-06-02 | PXD033042 | Pride

Proteomic identification of IqgC binding partners

Project description:Putative binding partners of IQGAP-related protein IqgC were identified by LC-MS/MS. Recombinant GST-tagged IqgC was purified from E. coli and immobilised to glutathione agarose. Interactors from cell lysate of D discoideum AX2 cells were applied to prepared affinity resin and bound proteins were identified by LC-MS/MS.

2018-12-21 | PXD006311 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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