Work

RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site

Year: 2023

Type: article

Abstract: (Cell Reports 37, 109934; November 2, 2021) In the originally published version of this paper, there were two unintentional errors in Figures 4 and S6. In Figure 4, the authors included cMYC staining from a different treatment group for Figure 4L for the shControl group. In Figure S6E, panels for proximity ligation assay for the group siFXR1 for cMYC probe-1 for Kuramochi cell line were inadvertently placed with the images of cMYC probe P2 panel of Kuramochi cell line from Figure S6D. Both figures have been corrected online and appear below. These corrections do not change the conclusions of the study, and the authors regret the errors. Figure 4Stable knockdown of FXR1 reduced the overall tumor growth, metastasis, and prolonged survival of ovarian xenograft mouse model (original)View Large Image Figure ViewerDownload Hi-res image Download (PPT)Figure S6FXR1 binds to the 3′UTRs within cMYC transcript, related to Figure 6 (corrected)View Large Image Figure ViewerDownload Hi-res image Download (PPT)Figure S6FXR1 binds to the 3′UTRs within cMYC transcript, related to Figure 6 (original)View Large Image Figure ViewerDownload Hi-res image Download (PPT) RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start siteGeorge et al.Cell ReportsNovember 02, 2021In BriefGeorge et al. demonstrate that FXR1 binds to the AREs within the 3′UTR of MYC mRNA and improves its stability. The authors also show that the RGG domain of FXR1 interacts with eIF4A1 and eIF4E and facilitates recruitment of the eIF4F complex to translation initiation sites for cMYC translation. Full-Text PDF Open Access

Source: Cell Reports

DOI: 10.1016/j.celrep.2023.112228