<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Li H</submitter><funding>National Key R&amp;amp;D Program of China</funding><funding>National Key R&amp;D Program of China</funding><funding>National Natural Science Foundation of China</funding><funding>Fok Ying Tung Education Foundation</funding><pagination>467</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11071816</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>79(8)</volume><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</pubmed_abstract><journal>Cellular and molecular life sciences : CMLS</journal><pubmed_title>Global phosphoproteomic analysis identified key kinases regulating male meiosis in mouse.</pubmed_title><pmcid>PMC11071816</pmcid><funding_grant_id>2021YFC2700200</funding_grant_id><funding_grant_id>82001611</funding_grant_id><funding_grant_id>81971439</funding_grant_id><funding_grant_id>161037</funding_grant_id><funding_grant_id>32071133</funding_grant_id><pubmed_authors>Yao L</pubmed_authors><pubmed_authors>Li H</pubmed_authors><pubmed_authors>Wang B</pubmed_authors><pubmed_authors>Guo Y</pubmed_authors><pubmed_authors>Guo X</pubmed_authors><pubmed_authors>Zhu H</pubmed_authors><pubmed_authors>Chen H</pubmed_authors><pubmed_authors>Zhao Y</pubmed_authors><pubmed_authors>Li Y</pubmed_authors><pubmed_authors>Cui Y</pubmed_authors><pubmed_authors>Ren J</pubmed_authors><pubmed_authors>Zhang X</pubmed_authors><pubmed_authors>Qi Y</pubmed_authors><pubmed_authors>Chen Y</pubmed_authors><pubmed_authors>Situ C</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Zhu T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Global phosphoproteomic analysis identified key kinases regulating male meiosis in mouse.</name><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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Aug</publication><modification>2026-06-01T08:06:14.251Z</modification><creation>2026-04-08T10:51:13.586Z</creation></dates><accession>S-EPMC11071816</accession><cross_references><pubmed>35930080</pubmed><doi>10.1007/s00018-022-04507-8</doi></cross_references></HashMap>