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 Sep 10;10(9):60. doi: 10.1038/s41389-021-00350-x

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

© The Author(s) 2021

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 4 — Western blotting of ESR1 (A, B) and SENP1 (B) levels in the indicated breast cancer cell lines. GAPDH was used as the loading control. A star represents SUMOylation of ESR1. C Estrogen response element (ERE) luciferase reporter activity was analyzed in the indicated cells treated with E2 (10 nM) and/or TAM (1 μM). Data are presented as the mean ± SD. *P < 0.05. D Immunoprecipitation assay revealing that TRIM3 interacts with ESR1, UBC9, and SAE1 in the indicated cells. E Schematic illustration of wild-type ESR1 and truncated ESR1. F Immunoprecipitation assay revealing that TRIM3 interacts with the ER2 domain of ESR1. G Far-western blotting revealing that TRIM3 directly interacts with Flag-ESR1 in the cell lysate.