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Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility
During sperm cryopreservation, the most significant phenotype of cryodamage is the decrease in sperm motility. Several proteomics studies have already been performed to search for key regulators at the protein level. However, sperm functions are known to be highly regulated by phosphorylation signal...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8521533/ https://www.ncbi.nlm.nih.gov/pubmed/34596222 http://dx.doi.org/10.1042/BSR20211326 |
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author | Wang, Jing Wang, Jing Wang, Min Hong, Renyun Tang, Shanshan Xu, Yuanhua Zhao, Xia Zhou, Tao Wang, Zibin Huang, Shaoping |
author_facet | Wang, Jing Wang, Jing Wang, Min Hong, Renyun Tang, Shanshan Xu, Yuanhua Zhao, Xia Zhou, Tao Wang, Zibin Huang, Shaoping |
author_sort | Wang, Jing |
collection | PubMed |
description | During sperm cryopreservation, the most significant phenotype of cryodamage is the decrease in sperm motility. Several proteomics studies have already been performed to search for key regulators at the protein level. However, sperm functions are known to be highly regulated by phosphorylation signaling. Here, we constructed a quantitative phosphoproteome to investigate the expression change of phosphorylated sites during sperm cryopreservation. A total of 3107 phosphorylated sites are identified and 848 of them are found to be significantly differentially expressed (DE). Bioinformatics analysis showed that the corresponding genes of these regulated sites are highly associated with sperm motility, providing a connection between the molecular basis and the phenotype of cryodamage. We then performed kinase enrichment analysis and successfully identified glycogen synthase kinase-3α (GSK3A) as the key kinase that may play an important role in the regulation of sperm motility. We further constructed a GSK3A centric network that could help us better understand the molecular mechanism of cryodamage in sperm motility. Finally, we also verified that GSK3A was abnormally activated during this process. The presented phosphoproteome and functional associations provide abundant research resources for us to learn the regulation of sperm functions, as well as to optimize the cryoprotectant for sperm cryopreservation. |
format | Online Article Text |
id | pubmed-8521533 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-85215332021-10-29 Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility Wang, Jing Wang, Jing Wang, Min Hong, Renyun Tang, Shanshan Xu, Yuanhua Zhao, Xia Zhou, Tao Wang, Zibin Huang, Shaoping Biosci Rep Post-Translational Modifications During sperm cryopreservation, the most significant phenotype of cryodamage is the decrease in sperm motility. Several proteomics studies have already been performed to search for key regulators at the protein level. However, sperm functions are known to be highly regulated by phosphorylation signaling. Here, we constructed a quantitative phosphoproteome to investigate the expression change of phosphorylated sites during sperm cryopreservation. A total of 3107 phosphorylated sites are identified and 848 of them are found to be significantly differentially expressed (DE). Bioinformatics analysis showed that the corresponding genes of these regulated sites are highly associated with sperm motility, providing a connection between the molecular basis and the phenotype of cryodamage. We then performed kinase enrichment analysis and successfully identified glycogen synthase kinase-3α (GSK3A) as the key kinase that may play an important role in the regulation of sperm motility. We further constructed a GSK3A centric network that could help us better understand the molecular mechanism of cryodamage in sperm motility. Finally, we also verified that GSK3A was abnormally activated during this process. The presented phosphoproteome and functional associations provide abundant research resources for us to learn the regulation of sperm functions, as well as to optimize the cryoprotectant for sperm cryopreservation. Portland Press Ltd. 2021-10-12 /pmc/articles/PMC8521533/ /pubmed/34596222 http://dx.doi.org/10.1042/BSR20211326 Text en © 2021 The Author(s). https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Post-Translational Modifications Wang, Jing Wang, Jing Wang, Min Hong, Renyun Tang, Shanshan Xu, Yuanhua Zhao, Xia Zhou, Tao Wang, Zibin Huang, Shaoping Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title | Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title_full | Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title_fullStr | Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title_full_unstemmed | Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title_short | Quantitative phosphoproteomics reveals GSK3A substrate network is involved in the cryodamage of sperm motility |
title_sort | quantitative phosphoproteomics reveals gsk3a substrate network is involved in the cryodamage of sperm motility |
topic | Post-Translational Modifications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8521533/ https://www.ncbi.nlm.nih.gov/pubmed/34596222 http://dx.doi.org/10.1042/BSR20211326 |
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