AGS3-dependent trans-Golgi network membrane trafficking is essential for compaction in mouse embryos.

Zheng-Wen Nie, Ying-Jie Niu, Wenjun Zhou, Dong-Jie Zhou, Ju-Yeon Kim, Xiang-Shun Cui

Journal of cell science 2020 Dec 07

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Activator of G-protein signaling 3 (AGS3, also known as GPSM1) regulates the trans-Golgi network. The AGS3 GoLoco motif binds to Gαi and thereby regulates the transport of proteins to the plasma membrane. Compaction of early embryos is based on the accumulation of E-cadherin (Cdh1) at cell-contacted membranes. However, how AGS3 regulates the transport of Cdh1 to the plasma membrane remains undetermined. To investigate this, AGS3 was knocked out using the Cas9-sgRNA system. Both trans-Golgi network protein 46 (TGN46, also known as TGOLN2) and transmembrane p24-trafficking protein 7 (TMED7) were tracked in early mouse embryos by tagging these proteins with a fluorescent protein label. We observed that the majority of the AGS3-edited embryos were developmentally arrested and were fragmented after the four-cell stage, exhibiting decreased accumulation of Cdh1 at the membrane. The trans-Golgi network and TMED7-positive vesicles were also dispersed and were not polarized near the membrane. Additionally, increased Gαi1 (encoded by GNAI1) expression could rescue AGS3-overexpressed embryos. In conclusion, AGS3 reinforces the dynamics of the trans-Golgi network and the transport of TMED7-positive cargo containing Cdh1 to the cell-contact surface during early mouse embryo development. © 2020. Published by The Company of Biologists Ltd.

Citation

Zheng-Wen Nie, Ying-Jie Niu, Wenjun Zhou, Dong-Jie Zhou, Ju-Yeon Kim, Xiang-Shun Cui. AGS3-dependent trans-Golgi network membrane trafficking is essential for compaction in mouse embryos. Journal of cell science. 2020 Dec 07;133(23)