Site-specific phosphorylation of Tau protein is associated with deacetylation of microtubules in mouse spermatogenic cells during meiosis

• Published in: FEBS letters Vol. 588; no. 11; pp. 2003 - 2008
• Main Authors: Inoue, Hiroki, Hiradate, Yuuki, Shirakata, Yoshiki, Kanai, Kenta, Kosaka, Keita, Gotoh, Aina, Fukuda, Yasuhiro, Nakai, Yutaka, Uchida, Takafumi, Sato, Eimei, Tanemura, Kentaro
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 29.05.2014
• Subjects: Acetylation; Animals; Male; Meiosis; Mice; Mice, Inbred C57BL; Microtubules - metabolism; Phosphorylation; Protein Processing, Post-Translational; Seminiferous Tubules - cytology; Seminiferous Tubules - metabolism; Spermatocytes - physiology; Spermatogenesis; Tau; tau Proteins - metabolism; Testis; Tubulin - metabolism; Testis; Tau; Meiosis; Spermatogenesis
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2014.04.021

•We indicated that Tau protein is expressed and phosphorylated in the testis.•Site-specific phosphorylation of the protein occurs in meiosis.•Tubulin deacetylation is coincident with phosphorylation of the protein.•We suggest that Tau protein may regulate microtubules in male mouse meiosis. Tau is one of the microtubule-associated proteins and a major component of paired helical filaments, a hallmark of Alzheimer’s disease. Its expression has also been indicated in the testis. However, its function and modification in the testis have not been established. Here, we analyzed the dynamics of phosphorylation patterns during spermatogenesis. The expression of Tau protein and its phosphorylation were shown in the mouse testis. Immunohistochemistry revealed that the phosphorylation was strongly detected during meiosis. Correspondingly, the expression of acetylated tubulin was inversely weakened during meiosis. These results suggest that phosphorylation of Tau protein contributes to spermatogenesis, especially in meiosis.