{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li H"],"funding":["National Key R&D Program of China","National Key R&D Program of China","National Natural Science Foundation of China","Fok Ying Tung Education Foundation"],"pagination":["467"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11071816"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["79(8)"],"pubmed_abstract":["Meiosis, a highly conserved process in organisms from fungi to mammals, is subjected to protein phosphorylation regulation. Due to the low abundance of phosphorylation, there is a lack of systemic characterization of phosphorylation regulation of meiosis in mammals. Using the phosphoproteomic approach, we profiled large-scale phosphoproteome of purified primary spermatocytes undergoing meiosis I, and identified 14,660 phosphorylation sites in 4419 phosphoproteins. Kinase-substrate phosphorylation network analysis followed by in vitro meiosis study showed that CDK9 was essential for meiosis progression to metaphase I and had enriched substrate phosphorylation sites in proteins involved in meiotic cell cycle. In addition, histones and epigenetic factors were found to be widely phosphorylated"],"journal":["Cellular and molecular life sciences : CMLS"],"pubmed_title":["Global phosphoproteomic analysis identified key kinases regulating male meiosis in mouse."],"pmcid":["PMC11071816"],"funding_grant_id":["2021YFC2700200","82001611","81971439","161037","32071133"],"pubmed_authors":["Yao L","Li H","Wang B","Guo Y","Guo X","Zhu H","Chen H","Zhao Y","Li Y","Cui Y","Ren J","Zhang X","Qi Y","Chen Y","Situ C","Wang Y","Zhu T"],"additional_accession":[]},"is_claimable":false,"name":"Global phosphoproteomic analysis identified key kinases regulating male meiosis in mouse.","description":"Meiosis, a highly conserved process in organisms from fungi to mammals, is subjected to protein phosphorylation regulation. Due to the low abundance of phosphorylation, there is a lack of systemic characterization of phosphorylation regulation of meiosis in mammals. Using the phosphoproteomic approach, we profiled large-scale phosphoproteome of purified primary spermatocytes undergoing meiosis I, and identified 14,660 phosphorylation sites in 4419 phosphoproteins. Kinase-substrate phosphorylation network analysis followed by in vitro meiosis study showed that CDK9 was essential for meiosis progression to metaphase I and had enriched substrate phosphorylation sites in proteins involved in meiotic cell cycle. In addition, histones and epigenetic factors were found to be widely phosphorylated","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-06-01T08:06:14.251Z","creation":"2026-04-08T10:51:13.586Z"},"accession":"S-EPMC11071816","cross_references":{"pubmed":["35930080"],"doi":["10.1007/s00018-022-04507-8"]}}