The PSMA8 subunit of the spermatoproteasome is essential for proper meiotic exit and mouse fertility

[EN]The ubiquitin proteasome system regulates meiotic recombination in yeast through its association with the synaptonemal complex, a ‘zipper’-like structure that holds homologous chromosome pairs in synapsis during meiotic prophase I. In mammals, the proteasome activator subunit PA200 targets acety...

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Bibliographic Details
Authors: Gómez-H, Laura, Felipe-Medina, Natalia, Condezo, Yazmine B., García-Valiente, Rodrigo, Ramos, Isabel, Suja, José Ángel, Barbero, José Luis, Roig, Ignasi, Sánchez Martín, Manuel Adolfo, de Rooij, Dirk G., Llano Cuadra, María Elena, Martín Pendás, Alberto
Format: article
Status:Published version
Publication Date:2019
Country:España
Institution:Universidad de Salamanca (USAL)
Repository:GREDOS. Repositorio Institucional de la Universidad de Salamanca
OAI Identifier:oai:gredos.usal.es:10366/146283
Online Access:http://hdl.handle.net/10366/146283
Access Level:Open access
Keyword:Spermatoproteasome
PSMA8
Mouse fertility
Homologous chromosome
DNA
Meiotic
Spermatocytes
Fertility
2409 Genética
ADN
fertilidad
espermatocitos
Description
Summary:[EN]The ubiquitin proteasome system regulates meiotic recombination in yeast through its association with the synaptonemal complex, a ‘zipper’-like structure that holds homologous chromosome pairs in synapsis during meiotic prophase I. In mammals, the proteasome activator subunit PA200 targets acetylated histones for degradation during somatic DNA double strand break repair and during histone replacement during spermiogenesis. We investigated the role of the testis-specific proteasomal subunit α4s (PSMA8) during spermatogenesis, and found that PSMA8 was localized to and dependent on the central region of the synaptonemal complex. Accordingly, synapsis-deficient mice show delocalization of PSMA8. Moreover, though Psma8-deficient mice are proficient in meiotic homologous recombination, there are alterations in the proteostasis of several key meiotic players that, in addition to the known substrate acetylated histones, have been shown by a proteomic approach to interact with PSMA8, such as SYCP3, SYCP1, CDK1 and TRIP13. These alterations lead to an accumulation of spermatocytes in metaphase I and II which either enter massively into apoptosis or give rise to a low number of aberrant round spermatids that apoptose before histone replacement takes place.

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