Systematic analysis of the ubiquitome in mouse testis.
histone
mouse
spermatogenesis
testis
ubiquitination
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
revised:
12
05
2021
received:
24
01
2021
accepted:
18
05
2021
pubmed:
30
5
2021
medline:
26
10
2021
entrez:
29
5
2021
Statut:
ppublish
Résumé
A growing body of evidence now supports the fact that protein ubiquitination is an important modification during the regulation of spermatogenesis. However, little is known about the ubiquitome of the testis. In this study, we created a large-scale mouse testis ubiquitome profile using di-glycine remnant antibodies and mass spectrometry and identified a total of 14,219 ubiquitination sites in 4217 proteins. Bioinformatics and phenotypic analyses showed that the ubiquitinated proteins were closely related to meiosis and spermiogenesis. And 512 ubiquitination regulatory enzymes were identified in testis that can exert regulatory functions over ubiquitination: the homologous to E6AP C-terminus (HECT) and multi-subunit RING-finger type E3 ligases were significantly enriched. In addition, we identified 22 new ubiquitination sites on testicular histones and 146 ubiquitinated epigenetic factors, thus demonstrating that ubiquitination plays an important role in epigenetic regulation. Collectively, this in-depth characterization of the ubiquitome in mouse testis could provide a rich resource for further studies of regulatory events at the protein level during spermatogenesis. All MS data are available via ProteomeXchange with the identifier PXD025866.
Identifiants
pubmed: 34050602
doi: 10.1002/pmic.202100025
doi:
Substances chimiques
Ubiquitinated Proteins
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2100025Informations de copyright
© 2021 Wiley-VCH GmbH.
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