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

Autor: Laura Gómez-H, Natalia Felipe-Medina, Yazmine B Condezo, Rodrigo Garcia-Valiente, Isabel Ramos, José Angel Suja, José Luis Barbero, Ignasi Roig, Manuel Sánchez-Martín, Dirk G de Rooij, Elena Llano, Alberto M Pendas
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: PLoS Genetics, Vol 15, Iss 8, p e1008316 (2019)
Druh dokumentu: article
ISSN: 1553-7390
1553-7404
DOI: 10.1371/journal.pgen.1008316
Popis: 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.
Databáze: Directory of Open Access Journals
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