Related Experiment Video
Updated: Feb 15, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
Human Papillomavirus E6 interaction with cellular PDZ domain proteins modulates YAP nuclear localization
Sydney Webb Strickland1, Nicole Brimer1, Charles Lyons1
1Department of Pathology, University of Virginia, Charlottesville, VA 22901, United States.
Human papillomavirus (HPV) oncoproteins, specifically E6, bind to cellular PDZ proteins, promoting the nuclear localization of YAP1. This interaction is a key mechanism by which E6 may contribute to cellular transformation.
Area of Science:
- Oncology
- Virology
- Molecular Biology
Background:
- Human papillomavirus (HPV) E6 oncoproteins are known to interact with cellular PDZ proteins.
- These interactions are crucial for understanding viral oncogenesis and cellular dysregulation.
Purpose of the Study:
- To identify novel cellular PDZ protein interactions with HPV16 and HPV18 E6 oncoproteins.
- To investigate the role of HPV E6-PDZ protein interactions in the regulation of YAP1 nuclear translocation.
Main Methods:
- Co-immunoprecipitation assays to identify E6-binding PDZ proteins.
- Western blotting to detect protein associations.
- Analysis of YAP1 localization in keratinocytes expressing HPV components.
Main Results:
- HPV16 E6 PBM associated with Dystrophin Glycoprotein Complex, LRCC1, and SLC9A3R2.
- HPV18 E6 showed additional associations with LRPPRC, RLGAPB, EIF3A, SMC proteins, AMOT, AMOTL1, and ARHGEF1 in adenomatous cell lines.
- E6 and E7 oncoproteins, and the complete HPV-16 genome, promoted YAP1 nuclear translocation in keratinocytes.
- E6's promotion of YAP1 nuclear transport required an intact PBM.
Conclusions:
- HPV E6 oncoproteins associate with a broader range of cellular PDZ proteins than previously known.
- E6-mediated PDZ protein interaction promotes YAP1 nuclear localization.
- This mechanism represents a potential pathway for HPV-driven cellular transformation.
More Related Videos
05:43A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
Published on: January 24, 2017
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
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Nuclear Localization Signals and Import
Conservation of Protein Domains
Nuclear Export of mRNA
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Nuclear Stability
To hold positively charged protons together...