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Proteome and phosphoproteome of Wip1-knockout mouse testis

ABSTRACT: 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. 90 proteins and 178 phosphoproteins 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis

SUBMITTER: yinghui wei

LAB HEAD: Yinghui Wei

PROVIDER: PXD008277 | Pride | 2022-03-01

REPOSITORIES: Pride

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Project description:Spermatogenesis is a complex cell differentiation process that includes marked genetic, cellular functional and structural changes. It requires tight regulation, since disturbances in any of the spermatogenic stages would lead to fertility deficiencies. In order to increase our knowledge of signal transduction during sperm development, we carried out a large-scale identification of the phosphorylation events that occur in the human gonad. Metal oxide affinity chromatography using TiOx combined with LC-MS/MS was conducted to profile the phosphoproteome of human testes with full spermatogenesis. A total of 8187 phosphopeptides derived from 2661 proteins were identified, resulting in the most complete report of human testicular phosphoproteins to date. Phosphorylation events were enriched in proteins functionally related to spermatogenesis, as well as to highly active processes in the male gonad, such as transcriptional and translational regulation, cytoskeleton organization, DNA packaging, cell cycle and apoptosis. Moreover, 174 phosphorylated kinases were identified. The most active and abundant human protein kinases in the testis were predicted both by the phosphorylation status of the kinase activation loop and the number of phosphopeptide spectra identified. The potential function of two of those kinases, cyclin-dependent kinase 12 (CDK12) and p21-activated kinase 4(PAK4), has been explored by protein-protein interaction analysis, immunodetection in human and mouse testicular tissue, and functional assay in a human embryonal carcinoma cell line. The co-localization of CDK12 with Golgi markers and probably pro-acrosomal vesicles suggests a potential crucial role of this protein kinase in sperm formation. PAK4 expression has been found limited to human spermatogonia, and a role in embryonal carcinoma cell response to apoptosis has been observed. Together, our data confirm that phosphoregulation by protein kinases is highly active in sperm differentiation, and open a window to detailed characterization and validation of potential targets for the development of drugs modulating male fertility, and tumor behavior.

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	MS-G3.raw	Raw

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Proteome and phosphoproteome of Wip1-knockout mouse testis

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