Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Phosphoproteome of mouse testis

ABSTRACT: Spermatogenesis is a complex sperm-generating process involving the mitosis of spermatogonia, meiosis of spermatocytes and spermiogenesis of spermatids. Elucidating the phosphorylation-based regulations should advance our understanding of the underlying molecular mechanisms. Here we present an integrative study of phosphorylation events in the testis. Large-scale phosphoproteome profiling in the adult mouse testis identified 17,829 phosphorylation sites in 3,955 phosphoproteins.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis

SUBMITTER: Tao Zhou

LAB HEAD: Jiahao Sha

PROVIDER: PXD000767 | Pride | 2014-10-10

REPOSITORIES: pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	maxquantresults.zip	Other
	mmtestis-5mg-SCX_ID9_6mm-IMACenriched-ql-0-1.mzXML	Mzxml
	mmtestis-5mg-SCX_ID9_6mm-IMACenriched-ql-0-2.mzXML	Mzxml
	mmtestis-5mg-SCX_ID9_6mm-IMACenriched-ql-1.mzXML	Mzxml
	mmtestis-5mg-SCX_ID9_6mm-IMACenriched-ql-10.mzXML	Mzxml

Items per page:

1 - 5 of 60

Publications

Systematic analysis of the phosphoproteome and kinase-substrate networks in the mouse testis.

Qi Lin L Liu Zexian Z Wang Jing J Cui Yiqiang Y Guo Yueshuai Y Zhou Tao T Zhou Zuomin Z Guo Xuejiang X Xue Yu Y Sha Jiahao J

Molecular & cellular proteomics : MCP 20141007 12

Spermatogenesis is a complex process closely associated with the phosphorylation-orchestrated cell cycle. Elucidating the phosphorylation-based regulations should advance our understanding of the underlying molecular mechanisms. Here we present an integrative study of phosphorylation events in the testis. Large-scale phosphoproteome profiling in the adult mouse testis identified 17,829 phosphorylation sites in 3955 phosphoproteins. Although only approximately half of the phosphorylation sites en ...[more]

PMID: 25293948

Similar Datasets

Protein phosphorylation landscape of mouse spermatids during spermiogenesis

Project description:Tadpole-shaped sperm is formed from round spermatid by spermiogenesis, a process with dramatic morphological changes in the final stage of spermatogenesis in testis. Protein phosphorylation, as one of the most important post-translational modifications, can regulate spermiogenesis, however, there is a lack of systemic analysis for phosphorylation events in this process. By large-scale phosphoproteome profiling using IMAC and TiO2 enrichment, we identified 18,980 phosphorylation sites in 4,628 phosphoproteins in mouse purified spermatids undergoing spermiogenesis. The identified phosphoproteins were significantly enriched in RNA transport, cell-cell adhesion, centrosome, microtubule and cilliogenesis. Further characterization of the kinase substrate relationship network demonstrated enrichment of phosphorylation substrates were related to the regulation of spermiogenesis. This global protein phosphorylation landscape of spermiogenesis showed wide phosphoregulation of diverse processes during spermiogenesis and could help further characterization of the process of sperm generation.

2019-03-29 | PXD011890 | Pride

TMT-based phosphoproteomics and proteomics analysis in Stk33-/- mouse testis

Project description:The phosphoproteome and proteome changes were quantified in Stk33-/- mouse testis using TMT 6-plex by LC-MS/MS.

2023-07-20 | PXD036903 | Pride

Phosphoproteome of a patient-matched cell line model of colon cancer metastasis

Project description:The contributions of phosphorylation-mediated signaling networks to colon cancer metastasis are poorly defined. To better understand the role of constitutive signaling alterations in cancer progression, the global phosphoproteomes of the SW480 and SW620 cell lines were compared by LC-MS/MS. These patient-matched cell lines were derived from a primary colon tumor and a lymph node metastasis, respectively. Network analysis of the significantly altered phosphosites revealed differential regulation in cellular adhesion, mitosis, and mRNA translational machinery. Among the latter group were sites on phosphoproteins with known roles in mRNA biogenesis and splicing, transport through the nuclear pores, initiating translation, as well as mRNA stability and degradation. Though alterations in these processes have been associated with oncogenic transformation, control of mRNA stability has typically not been associated with cancer progression. Notably, the single phosphosite with the greatest relative change in SW620 was Ser2 on eIF2S2, suggesting that SW620 cells translate faster or with greater efficiency than SW480 cells. These broad changes in the regulation of translation also occur without over-expression of eIF4E. Altogether, this work shows that metastatic cells exhibit constitutive changes to the phosphoproteome, and that mRNA stability and translational efficiency may be important targets of deregulation during cancer progression.

2017-01-06 | PXD003708 | Pride

In-depth Endogenous Phosphopeptidomics of Serum with Zirconium (IV)-Grafted Mesoporous Silica Enrichment

Project description:In this study, we developed an approach using Zirconium (IV)-grafted mesoporous beads to enrich phosphopeptides followed by analysis with a high resolution nanoRPLC-MS/MS system. The new method was first tested with tryptic digests of standard phosphoproteins and HeLa cell lysates, with excellent enrichment performance achieved. The method was further used for endogenous phosphopeptidomic analysis of serum samples from pancreatic ductal adenocarcinoma (PDAC) patients and controls. In total, 329 endogenous phosphopeptides (containing 113 high confidence sites) were identified across samples, by far the largest endogenous phosphorylation dataset catalogued to date. In addition, the method was readily applied for phosphoproteomics of the same set of samples, with 172 phosphopeptides identified and significant changes in dozens of phosphopeptides observed. Taken together, this method serves as a benchmark for analyzing serum phosphorylation events. Given the simplicity and robustness of the proposed method, we envision that it can be readily used for comprehensive phosphorylation studies (i.e., simultaneous endogenous phosphopeptidomics and phosphoproteomics) of serum and other biofluid samples.

2024-06-16 | PXD045146 | Pride

Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion

Project description:Our understanding of the key phosphorylation-dependent signalling pathways in the human malaria parasite, Plasmodium falciparum, remains rudimentary. Here we address this issue for the essential cGMP-dependent protein kinase, PfPKG. By employing chemical and genetic tools in combination with quantitative global phosphoproteomics, we identify the phosphorylation sites on 69 proteins that are direct or indirect cellular targets for PfPKG. These PfPKG targets include proteins involved in cell signalling, proteolysis, gene regulation, protein export and ion and protein transport, indicating that cGMP/PfPKG acts as a signalling hub that plays a central role in a number of core parasite processes. We also show that PfPKG activity is required for parasite invasion. This correlates with the finding that the calcium-dependent protein kinase, PfCDPK1, is phosphorylated by PfPKG, as are components of the actomyosin complex, providing mechanistic insight into the essential role of PfPKG in parasite egress and invasion.

2017-09-22 | PXD002266 | Pride

Large-scale Proteomic and Phosphoproteomic Analysis of Maize Seedling Leaves During De-etiolation

Project description:De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light. During this process light, an important environmental signal, triggers the inhibition of mesocotyl elongation and the production of photosynthetically active chloroplasts, and etiolated leaves transition from the “sink” stage to the “source” stage. De-etiolation has been extensively studied in maize (Zea mays L). However, little is known about how this transition is regulated. In this study, we describe a quantitative proteomic and phosphoproteomic atlas of the de-etiolation process in maize. We identified 16,420 proteins and quantified 14,168. In addition, 8,746 phosphorylation sites within 3,110 proteins were identified. From the proteomic and phosphoproteomic data combined, we identified a total of 17,436 proteins, 27.6% of which are annotated protein coding genes in the Zea_mays AGPv3.28 database. Only 6% of proteins significantly changed in abundance during de-etiolation. In contrast, the phosphorylation levels of more than 25% of phosphoproteins significantly changed; these included proteins involved in gene expression and homeostatic pathways and rate-limiting enzymes involved in photosynthesis light and carbon reactions. Based on phosphoproteomic analysis, 34% (1,057) of all phosphoproteins identified in this study contained more than three phosphorylation sites, and 37 proteins contained more than 16 phosphorylation sites, which shows that multi-phosphorylation is ubiquitous during the de-etiolation process. Our results suggest that plants might preferentially regulate the level of PTMs rather than protein abundance for adapting to changing environments. The study of PTMs could thus better reveal the regulation of de-etiolation.

2020-04-09 | PXD012897 | Pride

Integrative proteomic and phosphoproteomic profiling of testis from Wip1-knockout mice: insights into mechanisms of reduced fertility

Project description:Spermatogenesis plays an important role in the mammalian testis, involving in the complex processes of mitosis, meiosis, and spermiogenesis. Spermatogenesis may also be disrupted in the absence of the immunological and ‘fence’ functions of the BTB, resulting in male subfertility or infertility. Mice lacking wild-type p53-induced phosphatase 1 (Wip1) display male reproductive organ defects, but the molecular mechanisms underlying these abnormalities remain unclear. We explored the function of Wip1 in spermatogenesis and fertility by examining differences in the expressed testis proteome and phosphoproteome between Wip1-deficient and wild-type mice using a proteomics approach. Among a total of 6872 proteins and 4280 phosphorylation sites on 1614 proteins identified in our analysis, 58 proteins and 159 phosphorylation sites on 141 proteins were differentially regulated between these two groups of mice. These results suggested that proinflammatory cytokines may impair the blood–testis barrier dynamics by decreasing the expression of junction-associated proteins, which effect could be partially responsible for the subfertility and spermatogenesis defects in Wip1-knockout mice.

2018-11-02 | PXD009220 | Pride

Complementary Phosphoproteomic Approaches Link IL-23R Downstream Signaling with Metabolic Adaptation in Lymphocytes

Project description:Interleukin (IL)-23 mediated signal transduction represents a major molecular mechanism underlying the pathology of inflammatory bowel disease (IBD), Crohn's disease (CD) and ulcerative colitis (UC). In addition, emerging evidence supports the role of IL-23-driven Th17 cells in inflammation. Components of the IL-23 signalling pathway, such as IL23R, JAK2 and STAT3, have been characterised, but elements unique to this network as compared to other interleukins have not been readily addressed. In this study, we have undertaken a multi-stage phosphoproteomics approach to better characterise downstream signalling events. To this end, we performed and compared phosphopeptide and phosphoprotein enrichment methodologies after activation of T lymphocytes by IL-23. We demonstrate the complementary nature of the two phosphor-enrichment approaches by maximising the capture of phosphorylation events. A total of 8069 unique phosphopeptides (containing 8344 unique sites), and 4317 unique phosphorylated proteins were identified, amongst which STAT3, PKM2, CDK6 and LASP-1 clearly showed induction of specific phosphorylation sites that were not readily observed after IL-2 stimulation. Interestingly, we observed subsequent translocation of STAT3 and PKM2 to the nucleus as well as increased phosphorylation especially of the nuclear portion at ~30 min after IL-23 stimulation, suggesting a wide range of cellular responses including proliferation and metabolic adaptation.

2016-04-21 | PXD002990 | Pride

Effect of Titanium dioxide nanoparticles on Escherichia coli K12 MG1655 genes expression

Project description:In the present study, we investigated the transcriptional expression patterns of the model strain E. coli exposed to titanium dioxide nanoparticles (NP-TiO2), under dark conditions by using a microarray. Expression profiles were compared to unexposed E.coli and ratio of expression were analysed. Cell exposure to NP-TiO2 was conducted in 10 mM NaCl, E. coli bacterial suspension and NP-TiO2 stock suspension (or mQ water for the control) were added to the NaCl solution to obtain final concentrations of 10E7 cells/ml and 100 mg/l of TiO2 nanoparticles. The flasks were then incubated at 20M-BM-0C on a dark rotary shaker for 5 h. Exposed NP-TiO2: 4 biological replicats. Control: 4 biological replicats.

2014-09-08 | E-GEOD-55972 | biostudies-arrayexpress

Macro-porous Reversed Phase Separation of Proteins Combined with Reversed Phase Separation of Phosphopeptides and Tandem Mass Spectrometry for Profiling the Phosphoproteome of MDA-MB-231 cells

Project description:A new method of combining macro-porous reversed phase (mRP) protein fractionation with reversed phase liquid chromatography (RPLC) peptide separation tandem mass spectrometry (MS/MS) is reported for profiling the phosphoproteome of a complex sample. In this method, an mRP-C18 column was used to fractionate the proteins from a whole cell lysate of a breast cancer cell line, MDA-MB-231, into 38 fractions. Each fraction was subjected to tryptic digestion, sequential phosphopeptide enrichment by immobilized metal ion affinity chromatography (IMAC) and titanium dioxide (TiO2), followed by capillary RPLC-MS/MS analysis. For comparison, the conventional method of using strong cation exchange (SCX)-RPLC separation of peptides combined with MS/MS was also used for analyzing the phosphoproteome. Replicate experiments by the mRP-RPLC method identified 1585 distinct phosphoproteins with 4519 phosphopeptides, compared to 1585 phosphoproteins with 4297 phosphopeptides by SCX-RPLC, with a total of 1947 phosphoproteins and 6278 phosphopeptides identified from the combined results. While the two methods have similar ability in the identification of the phosphoproteome, they produce complementary information. The phosphoproteins identified in this study, including 67 novel phosphorylation sites from 56 breast cancer related proteins, can serve as the entry point for future validation with biological implications in breast cancer.

2014-07-24 | PXD000948 | Pride