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p53 Forms Redox-Dependent Protein-Protein Interactions through Cysteine 277
Tao Shi1, Paulien E Polderman1, Marc Pagès-Gallego1
1Center for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands.
Antioxidants (Basel, Switzerland)
|October 23, 2021
Summary
The tumor suppressor p53 forms disulfide bonds with other proteins under oxidizing conditions. Cysteine 277 is critical for these interactions, which may fine-tune p53 activity in redox signaling.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Signaling
Background:
- Reversible cysteine oxidation is crucial for redox signaling, impacting protein function.
- The tumor suppressor p53 is redox-sensitive and its activity is regulated by post-translational modifications and protein interactions.
Purpose of the Study:
- To investigate whether p53 forms intermolecular disulfides with interacting proteins.
- To determine if these redox-dependent interactions contribute to p53 regulation.
Main Methods:
- Co-immunoprecipitation
- Quantitative mass spectrometry
- Western blot analysis
Main Results:
- p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions.
- Cysteine 277 of p53 is essential for most of these disulfide-dependent interactions.
- Identified interaction partners include 14-3-3θ and 53BP1.
Conclusions:
- p53 engages in disulfide-dependent interactions with other proteins.
- Cysteine 277 plays a key role in mediating these redox-dependent protein associations.
- These interactions likely contribute to the fine-tuning of p53 activity in response to cellular redox states.
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