Related Experiment Video
Updated: May 3, 2026

NF-κB-dependent Luciferase Activation and Quantification of Gene Expression in Salmonella Infected Tissue Culture Cells
Published on: January 12, 2020
Ribosomal protein S3 interacts with the NF-κB inhibitor IκBα
Tamsyn Stanborough1, Johannes Niederhauser1, Barbara Koch1
1Institut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Abstract:
Ribosomal protein S3 (RPS3) is part of nuclear, transcriptionally active and cytoplasmic inhibitory complexes containing NF-κB variant p65. We show that in resting HEK293 cells, RPS3 interacts with NF-κB inhibitor IκBα. In contrast, efficient co-precipitation of p65 with RPS3 was only achieved in the presence of ectopic IκBα. In addition, a strong in vitro interaction was observed between RPS3 and IκBα, while binding between RPS3 and p65 was very weak. Furthermore, IκBα facilitated the reconstitution of p65 and RPS3 into one complex in vitro. Our results suggest that IκBα sequesters not only p65 but also RPS3 in the cytoplasm. This would ensure maintenance of an RPS3 pool for the NF-κB pathway as well as equimolar release of RPS3 and p65 upon stimulation.
More Related Videos
11:27A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
Published on: November 2, 2018
10:05Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
Published on: January 16, 2017
Related Concept Videos
NF-κB-dependent Signaling Pathway
NF-κB-dependent Signaling Mechanism
The...
Regulation of Nuclear Protein Sorting
Co-activators and Co-repressors
Regulation of the Unfolded Protein Response
NF-kB-dependent Signaling Pathway
The JAK-STAT Signaling Pathway