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Analysis of EYA3 phosphorylation by Src kinase

ABSTRACT: Data-dependent nLC-MS/MS analysis of EYA3 phosphorylation by Src protein tyrosine kinase

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Aura Elena Ionescu

LAB HEAD: Stefan Eugen Szedlacsek

PROVIDER: PXD016526 | Pride | 2019-12-17

REPOSITORIES: Pride

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			Action	DRS
	080816_D311N_SRC_0h__run01.raw	Raw
	080816_D311N_SRC_0h__run01Area-01.msf	Msf
	080816_D311N_SRC_0h__run01Area.msf	Msf
	080816_D311N_SRC_2hEDWT__run01.raw	Raw
	080816_D311N_SRC_2hEDWT__run01Area.msf	Msf

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Publications

Analysis of EYA3 Phosphorylation by Src Kinase Identifies Residues Involved in Cell Proliferation.

Ionescu Aura E AE Mentel Mihaela M Munteanu Cristian V A CVA Sima Livia E LE Martin Eliza C EC Necula-Petrareanu Georgiana G Szedlacsek Stefan E SE

International journal of molecular sciences 20191213 24

Eyes absent (EYA) are non-thiol-based protein tyrosine phosphatases (PTPs) that also have transcriptional co-activator functions. Their PTP activity is involved in various pathologies. Recently, we demonstrated that Src tyrosine kinase phosphorylates human EYA3 by controlling its subcellular localization. We also found EYA3's ability to autodephosphorylate, while raising the question if the two opposing processes could be involved in maintaining a physiologically adequate level of phosphorylatio ...[more]

PMID: 31847183

Similar Datasets

Analysis of EYA3 phosphorylation by Src kinase

Project description:Data-dependent nLC-MS/MS analysis of EYA3 phosphorylation by Src protein tyrosine kinase

2019-12-17 | PXD016518 | Pride

Analysis of EYA3 phosphorylation by Src kinase

Project description:Data-dependent nLC-MS/MS analysis of EYA3 phosphorylation by Src protein tyrosine kinase

2019-12-17 | PXD016520 | Pride

Analysis of EYA3 phosphorylation by Src kinase

Project description:Native MS analysis of prokaryotically expressed and purified EYA3. Native MS analysis of EYA3 phosphorylation by Src and EYA3 autodephosphorylation reaction.

2019-12-17 | PXD016596 | Pride

Analysis of EYA3 phosphorylation by Src kinase

Project description:Data-dependent nLC-MS/MS analysis of EYA3 phosphorylation by Src protein tyrosine kinase

2019-12-17 | PXD016532 | Pride

Multiple functions for Eya3 in mammalian organism

Project description:The important function of Eya (eyes absent) in eye development of D.melanogaster is well known, the function of its mammalian orthologs Eya1-4 is only partially understood. Yet, no phenotype for Eya2 and Eya3 in humans or mouse have been described. In our study we analysed new Eya-deficient mouse model generated by insertional mutagenesis. Expression analysis of Eya3 by in-situ hybridizations and β-Gal-staining revealed a broad expression of the gene throughout development, e.g. in brain, eyes, branchial arches, somites and limbs. This diverse expression pattern suggests pleiotropic effects of Eya3 in mammalian organisms. In contrast to D. melanogaster, a close examination of the eye by various methods did not show any obvious ocular defects in mutant animals. A broad phenotypical characterization of homozygous mutants displayed decreased body weight and body length. Additionally, behavioral changes as a educed forward locomotor activity and altered exploratory behaviour were identified. A significant reduction of forelimb grip strength and an impairment of cardiac processes in Eya3-/- mice suggest a role for Eya3 in muscle development and heart function. Our results implicate that Eya3 plays various roles outside the eye with effects particularly on heart and muscle function in the mouse. Keywords: Eya3-deficient mice, cDNA microarrays, brain, heart, muscle

2008-12-17 | GSE9999 | GEO

Multiple functions for Eya3 in mammalian organism

Project description:The important function of Eya (eyes absent) in eye development of D.melanogaster is well known, the function of its mammalian orthologs Eya1-4 is only partially understood. Yet, no phenotype for Eya2 and Eya3 in humans or mouse have been described. In our study we analysed new Eya-deficient mouse model generated by insertional mutagenesis. Expression analysis of Eya3 by in-situ hybridizations and M-NM-2-Gal-staining revealed a broad expression of the gene throughout development, e.g. in brain, eyes, branchial arches, somites and limbs. This diverse expression pattern suggests pleiotropic effects of Eya3 in mammalian organisms. In contrast to D. melanogaster, a close examination of the eye by various methods did not show any obvious ocular defects in mutant animals. A broad phenotypical characterization of homozygous mutants displayed decreased body weight and body length. Additionally, behavioral changes as a educed forward locomotor activity and altered exploratory behaviour were identified. A significant reduction of forelimb grip strength and an impairment of cardiac processes in Eya3-/- mice suggest a role for Eya3 in muscle development and heart function. Our results implicate that Eya3 plays various roles outside the eye with effects particularly on heart and muscle function in the mouse. Keywords: Eya3-deficient mice, cDNA microarrays, brain, heart, muscle analysis of 4 Eya3 mutant mice versus a pool of 5 wildtype animals; brain, heart, and muscle; 8 hybridisations for each tissue: two technical replicates for each mutant animal including one dye-swap experiments

2008-12-17 | E-GEOD-9999 | biostudies-arrayexpress

Proteomic analysis of Eya3 binding partners

Project description:Eyes absent homolog 3 (EYA3) is a transcriptional cofactor that is known to partner with the sine oculis homeobox (SIX) family to regulate gene expression. In this study, we characterized a novel splice isoform of EYA3, including the alternative cassette exon 7 (EYA3+ex7), that becomes more highly expressed compared to the isoform lacking exon 7 (EYA3Δex7) during muscle cell differentiation and muscle development. This developmentally-regulated splicing pattern was evolutionarily conserved in humans, mice, rats, chickens, and zebrafish. We found that EYA3 isoforms are vital to proliferation and differentiation of myoblasts in a cell culture model of myogenesis. To understand the underlying mechanism, we defined the transcriptional networks controlled by EYA3 through RNA-sequencing of EYA3 depleted cells. We then hypothesized that binding partners of EYA3+ex7 and EYA3Δex7 might contribute to the mechanism by which they regulate transcription. An affinity-purification mass spectrometry approach was used to identify binding partners of EYA3 isoforms by heterologous expression of hemagglutinin (HA) tagged isoforms in HEK293T cells. 26 binding partners (defined as those with log2(FC) > 1 and p < 0.05 compared to HA epitope tag control) were shared among the EYA3 isoforms, including five transcription factors: zinc finger and BTB domain containing 1 (ZBTB1), tumor protein p53 (TP53), SIX5, SIX2, and SIX4. We next demonstrated that ZBTB1 and SIX4 share overlapping transcriptional targets with EYA3, indicating that EYA3 partners with ZBTB1 or SIX4 to regulate gene expression. Three and thirteen unique binding partners were discovered for EYA3Δex7 and EYA3+ex7, respectively. Therefore, inclusion of Eya3 exon 7 may allow for unique interactions and contribute to functions of EYA3+ex7 that are distinct from EYA3Δex7. This dataset includes affinity purified data for Eya3 isoforms in HEK293T cells.

2023-10-13 | PXD037572 | Pride

RNA-sequencing of differentiated mouse skeletal muscle cells following the depletion of EYA3

Project description:Mouse skeletal muscle cells were subjected to treatment with siRNAs targeting EYA3 or a non-targeting siRNA (si-Ctrl). Differential gene expression analysis was performed on the resulting data.

2023-10-06 | GSE212436 | GEO

Individual SRC-2 and SRC-3 knock-down in MCF-7 cells

Project description:Experimental aim: identification of SRC-2 and SRC-3-related genes in MCF-7 breast cancer cells. Experimental workflow: 1. shRNA transduction. MCF-7 cells were transduced with a mix of lentiviral particles containing five individual lentiviral pLKO.1-puro short hairpin (sh) RNA plasmids targeting different sequences on SRC-2 or SRC-3 mRNA and a pLKO.1-puro empty vector control. The puromycin selections were maintained for three weeks to obtain cells containing stably integrated shRNA. 2. Sample preparation. RNA was extracted from eight independent replicates expressing the pLKO.1-puro empty shRNA vector (shKTR), from eight replicates of SRC-2 shRNA expressing cells (shSRC-2), and from seven replicates of SRC-3 shRNA expressing cells (shSRC-3). 300 ng of total RNA from each cell sample was biotin-labelled and amplified.

2019-07-01 | E-MTAB-7018 | biostudies-arrayexpress

Systematic Identification of SHP2 Phosphatase Substrates

Project description:Phosphatases play essential roles in normal cell physiology and diseases like cancer. The challenges of studying phosphatases have limited our understanding of their substrates, molecular mechanisms, and unique functions within highly complicate networks. Here we introduce a novel strategy using substrate trapping mutant coupled with quantitative mass spectrometry to identify physiological substrates of protein tyrosine phosphatase Src homology 2 containing protein tyrosine phosphatase 2 (SHP2) in a high-throughput manner. SHP2 plays a critical role in numerous cellular processes through the regulation of various signaling pathways. The method integrates three separate MS-based experiments; in vitro dephosphorylation assay, in vivo global phosphoproteomics, and pull down of substrate trapping mutant complex using HEK293SHP2KO cells. PTPN11-C459S/D425A is an optimized substrate trap mutant of SHP2. We identified eleven direct substrates, including both known and novel SHP2 substrates in EGFR signaling pathways, among which docking protein 1 (DOK1) was further validated as a new SHP2 substrate. This advanced workflow significantly improves the systemic identification of direct substrates of phosphatase, facilitating the comprehension of equally important roles of phosphatase signaling.

2022-09-20 | PXD028404 | Pride

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