着丝粒配对对于减数分裂中的突触至关重要。本研究深入研究了Skp1-Cullin1-F-box蛋白(SCF)E3泛素连接酶复合物,特别关注F-box蛋白47(FBXO47),小鼠减数分裂。这里,我们发现,FBXO47位于着丝粒,它与SKP1协同调节着丝粒配对,以确保囊中的适当突触。缺乏FBXO47会导致着丝粒缺陷,导致着丝粒配对不完整,导致SC在着丝粒末端和沿着染色体轴的腐败,引发染色体过早解离和粗线质阻滞。FBXO47缺陷型粗线质精母细胞在着丝粒和染色体上的SKP1表达急剧下降。此外,FBXO47通过下调其在HEK293T细胞中的泛素化来稳定SKP1。实质上,我们建议FBXO47与SKP1合作促进精母细胞中着丝粒SCF的形成。总之,我们认为着丝粒SCFE3连接酶复合物调节着丝粒配对以促进小鼠的囊性进展。
Centromere pairing is crucial for synapsis in
meiosis. This study delves into the Skp1-Cullin1-F-box protein (SCF) E3 ubiquitin ligase complex, specifically focusing on F-box protein 47 (FBXO47), in mouse
meiosis. Here, we revealed that FBXO47 is localized at the centromere and it regulates centromere pairing cooperatively with SKP1 to ensure proper synapsis in pachynema. The absence of FBXO47 causes defective centromeres, resulting in incomplete centromere pairing, which leads to corruption of SC at centromeric ends and along chromosome axes, triggering premature dissociation of chromosomes and pachytene arrest. FBXO47 deficient pachytene spermatocytes exhibited drastically reduced SKP1 expression at centromeres and chromosomes. Additionally, FBXO47 stabilizes SKP1 by down-regulating its ubiquitination in HEK293T cells. In essence, we propose that FBXO47 collaborates with SKP1 to facilitate centromeric SCF formation in spermatocytes. In summary, we posit that the centromeric SCF E3 ligase complex regulates centromere pairing for pachynema progression in mice.