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Nakajo, M.

Publications and source records attributed to Nakajo, M..

2 recordsLinked to original sources

Sexual receptivity increases in synchrony with the ovulatory cycle in female medaka

Successful reproduction requires coordinated regulation of gonadal function and sexual behavior. However, the mechanisms of such a regulation remain elusive. Here, we used a teleost medaka to find out possible involvement of ovulation in the control of female sexual behaviors by analyzing the sexual behaviors of the female gene-knockout medaka that do not ovulate and found that ovulation is essential for the facilitation of female sexual receptivity. Behavioral recordings and anatomical examinations showed that the sexual behavior of medaka occurs only after the ovulation. Furthermore, progesterone administration partially reinstated the sexual receptivity of the anovulatory knockout females. Taken together with the result that progesterone receptor is expressed in the brain regions that are considered strong candidate for regulation of sexual behavior, we propose that female sexual receptivity is facilitated in synchrony with the ovulatory cycle via progesterone receptor signaling in specific brain regions that occurs around the timing of ovulation.

physiology↗

Centrosome maturation requires phosphorylation-mediated sequential domain interactions of SPD-5

Centrosomes consist of two centrioles and surrounding pericentriolar material (PCM). PCM expands during mitosis in a process called centrosome maturation, in which PCM scaffold proteins play pivotal roles to recruit other centrosomal proteins. In C. elegans, the scaffold protein SPD-5 forms PCM scaffold in a PLK-1 phosphorylation-dependent manner. However, how phosphorylation of SPD-5 promotes PCM scaffold assembly is unclear. Here, we identified three functional domains of SPD-5 through in vivo domain analyses, and propose that sequential domain interactions of SPD-5 are required for mitotic PCM scaffold assembly. Firstly, SPD-5 is targeted to centrioles through direct interaction between its centriole localization (CL) domain and a centriolar protein PCMD-1. Then, intra- and inter-molecular interaction between SPD-5 phospho-regulated multimerization (PReM) domain and the PReM association (PA) domain is triggered by phosphorylation by PLK-1, which leads to PCM scaffold expansion. Our findings suggest that the sequential domain interactions of scaffold proteins mediated by Polo/PLK-1 phosphorylation is an evolutionarily conserved mechanism of PCM scaffold assembly.

cell biology↗