PP1 forms an active complex with TLRR (lrrc67), a putative PP1 regulatory subunit, during the early stages of spermiogenesis in mice.
PP1 forms an active complex with TLRR (lrrc67), a putative PP1 regulatory subunit, during the early stages of spermiogenesis in mice.
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DOI：
10.1371/journal.pone.0021767
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发表时间：
2011
期刊：
影响因子：
3.7
通讯作者：
Sperry AO
中科院分区：
文献类型：
--
作者：
Wang R;Sperry AO
哺乳动物精子发生是一种高度调控的发育途径，需要雄性生殖细胞细胞骨架的戏剧性重排。我们已经描述了一个富含亮氨酸的重复蛋白TLRR(也称为lrrc67)，它与小鼠睾丸中的精子细胞骨架相关，是蛋白质磷酸酶-1(PP1)的结合伙伴，蛋白磷酸酶-1是一个非常保守的信号分子。PP1的活性受到许多特定调控因子的调节，TLRR是其中的候选调节因子。在这项研究中，我们测量了TLRR-PP1复合体在成年和发育中的小鼠睾丸中的磷酸酶活性，其中包含不同发育中的生殖细胞类型，以确定TLRR是作为PP1的激活剂还是抑制物，以及该复合体的磷酸酶活性在精子发生过程中是否受到发育调节。此外，我们还检测了细菌表达的TLRR对PP1酶活性的影响。此外，我们还检测了在发育中的睾丸的第一波精子发生过程中TLRR的磷酸化，以及精子细胞细胞骨架的成分。我们在这里证明了TLRR复合体与成年小鼠睾丸中的一种磷酸酶活性有关。这种复合体的相对磷酸酶活性在出生后21d左右达到高峰，此时小鼠睾丸生精上皮中有丰富的粗线型精母细胞和圆形精细胞。TLRR除了微管蛋白和动蛋白-1B外，还在精子发生的第一波中被磷酸化。这些发现表明，TLRR-PP1复合体在TLRR向精子鞭毛移位之前是活跃的，TLRR和精子细胞细胞骨架的成分在小鼠睾丸精子发生过程中可能受到可逆磷酸化的调节。
Mammalian spermatogenesis is a highly regulated developmental pathway that demands dramatic rearrangement of the cytoskeleton of the male germ cell. We have described previously a leucine rich repeat protein, TLRR (also known as lrrc67), which is associated with the spermatid cytoskeleton in mouse testis and is a binding partner of protein phosphatase-1 (PP1), an extremely well conserved signaling molecule. The activity of PP1 is modulated by numerous specific regulators of which TLRR is a candidate. In this study we measured the phosphatase activity of the TLRR-PP1 complex in the adult and the developing mouse testis, which contains varying populations of developing germ cell types, in order to determine whether TLRR acts as an activator or an inhibitor of PP1 and whether the phosphatase activity of this complex is developmentally regulated during spermatogenesis. Additionally, we assayed the ability of bacterially expressed TLRR to affect the enzymatic activity of PP1. Furthermore, we examined phosphorylation of TLRR, and elements of the spermatid cytoskeleton during the first wave of spermatogenesis in the developing testis. We demonstrate here that the TLRR complex is associated with a phosphatase activity in adult mouse testis. The relative phosphatase activity of this complex appears to reach a peak at about 21 days after birth, when pachytene spermatocytes and round spermatids are abundant in the seminiferous epithelium of the mouse testis. TLRR, in addition to tubulin and kinesin-1B, is phosphorylated during the first wave of spermatogenesis. These findings indicate that the TLRR-PP1 complex is active prior to translocation of TLRR toward the sperm flagella and that TLRR, and constituents of the spermatid cytoskeleton, may be subject to regulation by reversible phosphorylation during spermatogenesis in murine testis.
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