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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...

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Autores principales: Wang, Jing, Wang, Min, Hong, Renyun, Tang, Shanshan, Xu, Yuanhua, Zhao, Xia, Zhou, Tao, Wang, Zibin, Huang, Shaoping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2021
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.
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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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