Premium
Site‐specific phosphorylation of Tau protein is associated with deacetylation of microtubules in mouse spermatogenic cells during meiosis
Author(s) -
Inoue Hiroki,
Hiradate Yuuki,
Shirakata Yoshiki,
Kanai Kenta,
Kosaka Keita,
Gotoh Aina,
Fukuda Yasuhiro,
Nakai Yutaka,
Uchida Takafumi,
Sato Eimei,
Tanemura Kentaro
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.021
Subject(s) - meiosis , phosphorylation , microtubule , acetylation , spermatogenesis , microbiology and biotechnology , tubulin , biology , protein phosphorylation , tau protein , immunohistochemistry , microtubule associated protein , biochemistry , medicine , endocrinology , gene , immunology , alzheimer's disease , disease , protein kinase a
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.