The post-translational modification of proteins by covalent attachment of ubiquitin molecules targets protein for degradation by 26S proteasome composed of a 20S core unit capped with one 19S regulatory complex on each side. Such event plays a key role in numerous cellular functions including spermatogenesis. It is conceivable that ubiquitination is involved in all phases of spermatogenesis and its destinated functions control various cellular activities in the testis, ranging from the mitotic spindle formation in germ cells to the structural formation of the spermatid flagella. In this review, we aim to summarize the recent findings in the study of ubiquitination in the testis. It also highlights specific areas for future research toward a better understanding of the precise physiological relationship between ubiquitin-mediated proteolysis and spermatogenesis. Furthermore, a thorough understanding of this system that can lead to developing new approaches for male contraception is discussed.
Keywords: Ubiquitination, reproduction, contraception, cell junctions, spermatogenesis
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