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 Jun 5;12(6):581. doi: 10.1038/s41419-021-03871-w

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. 2 — A HuR-GST interacts with Pirh2. GST-pulldown assay with extracts from HEK293T, demonstrating the interaction of HuR-GST with Pirh2. A Ponceau-stained membrane. HuR-GST fusion protein and native GST protein are denoted with arrows (left); western blot analysis of Pirh2 binding to GST and HuR-GST (right). B Identification of the Pirh2 domains involved in HuR binding. WB analysis of GSTpull-down assay with purified GST-tagged proteins: GST, full-length Pirh2 (Pirh2-GST), the N-terminal domain of Pirh2 1–132 a.a. (NTD-GST), the RING domain of Pirh2 138–189 a.a. (RING-GST), and the C-terminal domain of Pirh2 190–261 a.a. (CTD-GST) (upper panel); the scheme demonstrating the Pirh2 domain structure (bottom panel). C Pirh2 interacts with HuR in cellulo. Western blot analysis of co-immunoprecipitation in HEK293T cells of ectopically expressed Pirh2-3×FLAG (pIRES-Pirh2) and endogenous HuR. An empty pIRES vector was used as negative control. D HuR interacts with Pirh2 in cellulo. Western blot analysis of co-immunoprecipitation in HeLa cells of ectopically expressed HuR-3×FLAG (pIRES-HuR) and endogenous Pirh2. An empty pIRES vector was used as negative control. E Co-immunoprecipitation of the endogenous HuR and Pirh2 proteins using anti-HuR monoclonal antibodies.