Dataset Information

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

ABSTRACT: Data from ProteomeXchange, PXD ID: PXD000767. Experiment: IMAC-1, file: mmtestis-5mg-SCX_ID9_6mm-IMACenriched-ql-0-2.mzXML. Published as part of Mol Cell Proteomics. 2014 Oct 7 . From the Abstract: {{i}} ... 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. Although only approximately half of the phosphorylation sites enriched by IMAC were also captured by TiO2, both the phosphoprotein datasets identified by the two methods significantly enriched the functional annotation of spermatogenesis ... {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Mus_musculus_viruses, Mouse

DISEASE(S): Not Available

SUBMITTER: Lin Qi, et al.

PROVIDER: GPM32320004513 | GPMDB |

REPOSITORIES: GPMDB

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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

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Project description:Background: Baylisascaris procyonis is an intestinal ascarid worm that parasitizes in raccoons and causes fatal neural, visceral, and ocular larva migrans in humans. Phosphorylated proteins and protein kinases have been studied as vaccine and drug target candidates against parasitic infections. However, no data are available on protein phosphorylation in the raccoon roundworm. Methods: In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phosphopeptides were enriched using immobilized metal affinity chromatography (IMAC) and analyzed by liquid chromatography-mass spectrometry (LC-MS/MS). Results: Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3,308 phosphopeptides total). The annotated phosphoproteins were associated with various biological processes, including cytoskeletal remodeling, supramolecular complex assembly, and developmental regulation. The phosphopeptide functional enrichment revealed that B. procyonis phosphoproteins were mostly involved in the cytoskeleton cellular compartment, protein binding molecular function, and multiple biological processes, including regulating supramolecular fiber and cytoskeleton organization, and assembling cellular protein-containing complexes and organelles. The significantly enriched pathways of phosphoproteins included the insulin signaling pathway, tight junction, endocytosis, longevity-regulating, glycolysis/gluconeogenesis, and apelin signaling pathways. Domain analysis revealed that the Src homology 3 domain was significantly enriched. Conclusions: This study presents the first phosphoproteomic landscape of B. procyonis, elucidating phosphorylation-mediated regulation of cytoskeletal dynamics, host interaction pathways, and metabolic adaptations. The identified 450 phosphoproteins and enriched functional domains establish a foundation for targeting conserved mechanisms critical to B. procyonis survival.

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Dataset Information

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

Publications

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

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