Mutual regulation between deubiquitinase CYLD and retroviral oncoprotein Tax
2011
How CYLD Regulates the Oncoprotein Tax in T-Cell Transformation
publication
Evidence: moderate
Author Information
Author(s): Wu Xuefeng, Zhang Minying, Sun Shao-Cong
Primary Institution: University of California at San Diego; The University of Texas MD Anderson Cancer Center
Hypothesis
How is the ubiquitination of the oncoprotein Tax regulated by the deubiquitinase CYLD?
Conclusion
CYLD negatively regulates the signaling function of Tax by inhibiting its ubiquitination, and its phosphorylation may allow HTLV1 to bypass this regulation.
Supporting Evidence
- CYLD physically interacts with Tax and inhibits its ubiquitination.
- Phosphorylation of CYLD in HTLV1-transformed T cells inactivates its deubiquitinating activity.
- Tax requires ubiquitination for its signaling function in the NF-κB pathway.
Takeaway
CYLD is like a brake that stops a bad protein called Tax from causing too much activity in cells, but HTLV1 can turn off this brake.
Methodology
The study involved co-immunoprecipitation and ubiquitination assays in various cell lines to analyze the interaction and regulation between CYLD and Tax.
Digital Object Identifier (DOI)
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