Role of FBXL5 in redox homeostasis and spindle assembly during oocyte maturation in mice

被引：1

作者：

Wang, Shiwei ^{[1
]}

Wu, Xuan ^{[1
]}

Wang, Han ^{[1
]}

Song, Shuang ^{[1
]}

Hu, Yuling ^{[1
]}

Guo, Yajun ^{[1
]}

Chang, Siyu ^{[1
]}

Cheng, Yuanweilu ^{[1
]}

Zeng, Shenming ^{[1
]}

机构：

[1] China Agr Univ, Coll Anim Sci & Technol, Natl Engn Lab Anim Breeding, Key Lab Anim Genet Breeding,Minist Agr, Beijing, Peoples R China

来源：

FASEB JOURNAL | 2023年 / 37卷 / 08期

关键词：

CITED2; FBXL5; mitochondria; oocyte quality; reproduction; BINDING-PROTEIN; F-BOX; CITED2; DEGRADATION; CELLS; GENE; IRON; AXIS;

D O I：

10.1096/fj.202300244RR

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

As an E3 ubiquitin ligase, F-box and leucine-rich repeat protein 5 (FBXL5) participates in diverse biologic processes. However, the role of Fbxl5 in mouse oocyte meiotic maturation has not yet been fully elucidated. The present study revealed that mouse oocytes depleted of Fbxl5 were unable to complete meiosis, as Fbxl5 silencing led to oocyte meiotic failure with reduced rates of GVBD and polar body extrusion. In addition, Fbxl5 depletion induced aberrant mitochondrial dynamics as we noted the overproduction of reactive oxygen species (ROS) and the accumulation of phosphorylated ?H2AX with Fbxl5 knockdown. We also found that Fbxl5-KD led to the abnormal accumulation of CITED2 proteins in mouse oocytes. Our in vitro ubiquitination assay showed that FBXL5 interacted with CITED2 and that it mediated the degradation of CITED2 protein through the ubiquitination-proteasome pathway. Collectively, our data revealed critical functions of FBXL5 in redox hemostasis and spindle assembly during mouse oocyte maturation.

引用

页数：13

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