Proteomics

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Quantitative phosphoproteomics analysis of GV, GVBD and MII oocytes

ABSTRACT: Five replicates of GV, GVBD, and MII oocytes were subjected to the 15-plex TMT labeling, HP-RP fractionation, and LC-MS/MS analysis. For each replicate, 2,000 oocytes were collected from each of the GV, GVBD, and MII stages. Ti4+-IMAC was used to enrich phosphopeptides.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Oocyte

SUBMITTER: Yueshuai Guo  

LAB HEAD: Xuejiang Guo

PROVIDER: PXD050645 | Pride | 2025-05-13

REPOSITORIES: Pride

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TMT15_mmOocyte_GV_GVBD_MII_HPRP_F10_20210201.raw Raw
TMT15_mmOocyte_GV_GVBD_MII_HPRP_F11_20210203.raw Raw
TMT15_mmOocyte_GV_GVBD_MII_HPRP_F12_20210203.raw Raw
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Publications

Phosphorylation is a key post-translational modification regulating protein function and biological outcomes. However, the phosphorylation dynamics orchestrating mammalian oocyte development remains poorly understood. In the present study, we apply high-resolution mass spectrometry-based phosphoproteomics to obtain the first global in vivo quantification of mouse oocyte phosphorylation. Of more than 8000 phosphosites, 75% significantly oscillate and 64% exhibit marked upregulation during meiotic  ...[more]

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