Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Jul 17;14:112. doi: 10.1186/s13045-021-01123-0

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

PMC Copyright notice

Fig. 5 — LCAT3 physically interacts with FUBP1. A Proteins interacting with LCAT3 were identified by pull down assay followed by mass spectrometry analysis. B Western blot analysis of FUBP1 in beads only, negative control, sense and antisense LCAT3 pull-down fractions. GAPDH served as a negative control. C. FUBP1 RIP assays in Calu1 cells. A western blot assay confirmed FUBP1 immunoprecipitation (Up); The relative fold enrichment of LCAT3 between FUBP1 and IgG RIP fractions was determined by qRT-PCR (Down). D LCAT3 sense and 208–342 nt fragments were performed with RNA pull down and western blotting assays. E The schematic structure of full-length FUBP1 proteins (FL: 1–644) and three domain-deleted mutants (MUT1: 100–644; MUT2: 1–100 and 447–644; MUT3: 1–511) of FUBP1 variants used in this study. The blue box is the inhibitory domain, the orange box is the DNA and RNA binding domain, and the purple box is the transcription domain. F RIP assays were performed using anti-FLAG antibodies in Calu1 cells that were transfected with vectors expressing the FLAG-tagged FL and the deleted mutants (MUT1-3) of FUBP1. G Relative mRNA expression of FUBP1 primary tumors (n = 515) and in adjacent normal tissues (n = 59) from TCGA LUAD samples. H Relative protein expression of FUBP1 in primary tumors (n = 111) and adjacent normal tissue (n = 111) from Clinical Proteomic Tumor Analysis Consortium (CPTAC) LUAD samples. I Kaplan–Meier survival analysis of overall survival of lung cancer patients using FUBP1 expression. The data were downloaded from the study of Takeuchi et al. (GEO accession: GSE11969; No. patients: 90)