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Proteomics. 2019 Mar 22:e1900055. doi: 10.1002/pmic.201900055. [Epub ahead of print]

The Protein Phosphorylation Landscape of Mouse Spermatids During Spermiogenesis.

Author information

1
State Key Laboratory of Reproductive Medicine, Department of Histology and Embryology, Nanjing Medical University, Nanjing, 210029, China.
2
Center of Pathology and Clinical Laboratory, Sir Run Run Hospital, Nanjing Medical University, Nanjing, Jiangsu, 211166, China.

Abstract

The characteristic tadpole-shape of sperm is formed from round spermatids via spermiogenesis, a process which results in dramatic morphological changes in the final stage of spermatogenesis in the testis. Protein phosphorylation, as one of the most important post-translational modifications, can regulate spermiogenesis; however, the phosphorylation events taking place during this process have not been systematically analyzed. In order to better understand the role of phosphorylation in spermiogenesis, we performed large-scale phosphoproteome profiling using IMAC and TiO2 enrichment. In total, 13,835 phosphorylation sites, in 4,196 phosphoproteins, were identified in purified mouse spermatids undergoing spermiogenesis in two biological replicates. Overall, 735 testis-specific proteins were identified to be phosphorylated, and were expressed at high levels during spermiogenesis. Gene ontology analysis showed enrichment of the identified phosphoproteins in terms of histone modification, cilium organization, centrosome and the adherens junction. Further characterization of the kinase-substrate phosphorylation network demonstrated enrichment of phosphorylation substrates related to the regulation of spermiogenesis. This global protein phosphorylation landscape of spermiogenesis showed wide phosphoregulation across a diverse range of processes during spermiogenesis and could help to further characterize the process of sperm generation. All MS data are available via ProteomeXchange with the identifier PXD011890. This article is protected by copyright. All rights reserved.

PMID:
30901149
DOI:
10.1002/pmic.201900055

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