TY - JOUR TI - RETRACTED: Arginine methylation of SHANK2 by PRMT7 promotes human breast cancer metastasis through activating endosomal FAK signalling AU - Liu, Yingqi AU - Li, Lingling AU - Liu, Xiaoqing AU - Wang, Yibo AU - Liu, Lingxia AU - Peng, Lu AU - Liu, Jiayuan AU - Zhang, Lian AU - Wang, Guannan AU - Li, Hongyuan AU - Liu, Dong-Xu AU - Huang, Baiqu AU - Lu, Jun AU - Zhang, Yu A2 - Postovit, Lynne-Marie A2 - White, Richard M A2 - Postovit, Lynne-Marie A2 - Mallette, Fred VL - 9 PY - 2020 DA - 2020/08/26 SP - e57617 C1 - eLife 2020;9:e57617 DO - 10.7554/eLife.57617 UR - https://doi.org/10.7554/eLife.57617 AB - Arginine methyltransferase PRMT7 is associated with human breast cancer metastasis. Endosomal FAK signalling is critical for cancer cell migration. Here we identified the pivotal roles of PRMT7 in promoting endosomal FAK signalling activation during breast cancer metastasis. PRMT7 exerted its functions through binding to scaffold protein SHANK2 and catalyzing di-methylation of SHANK2 at R240. SHANK2 R240 methylation exposed ANK domain by disrupting its SPN-ANK domain blockade, promoting in co-accumulation of dynamin2, talin, FAK, cortactin with SHANK2 on endosomes. In addition, SHANK2 R240 methylation activated endosomal FAK/cortactin signals in vitro and in vivo. Consistently, all the levels of PRMT7, methylated SHANK2, FAK Y397 phosphorylation and cortactin Y421 phosphorylation were correlated with aggressive clinical breast cancer tissues. These findings characterize the PRMT7-dependent SHANK2 methylation as a key player in mediating endosomal FAK signals activation, also point to the value of SHANK2 R240 methylation as a target for breast cancer metastasis. KW - metastasis KW - endocytosis KW - methylation KW - PRMT7 KW - SHANK2 KW - FAK JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -