| Literature DB >> 27994054 |
Yi Xiao1,2, Haixia Ma1,2, Ping Wan3, Dandan Qin1,2, Xiaoxiao Wang1,2, Xiaoxin Zhang1, Yunlong Xiang1, Wenbo Liu1, Jiong Chen4, Zhaohong Yi5, Lei Li6,2.
Abstract
Trp-Asp (WD) repeat domain 1 (WDR1) is a highly conserved actin-binding protein across all eukaryotes and is involved in numerous actin-based processes by accelerating Cofilin severing actin filament. However, the function and the mechanism of WDR1 in mammalian early development are still largely unclear. We now report that WDR1 is essential for mouse peri-implantation development and regulates Cofilin phosphorylation in mouse cells. The disruption of maternal WDR1 does not obviously affect ovulation and female fertility. However, depletion of zygotic WDR1 results in embryonic lethality at the peri-implantation stage. In WDR1 knock-out cells, we found that WDR1 regulates Cofilin phosphorylation. Interestingly, WDR1 is overdosed to regulate Cofilin phosphorylation in mouse cells. Furthermore, we showed that WDR1 interacts with Lim domain kinase 1 (LIMK1), a well known phosphorylation kinase of Cofilin. Altogether, our results provide new insights into the role and mechanism of WDR1 in physiological conditions.Entities:
Keywords: Limk1; WDR1; actin; cofilin; development; embryonic development; mouse genetics; phosphorylation
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Year: 2016 PMID: 27994054 PMCID: PMC5270486 DOI: 10.1074/jbc.M116.759886
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157