HDAC3 as a Molecular Chaperone for Shuttling Phosphorylated TR2 to PML: A Novel Deacetylase Activity-Independent Function of HDAC3
2009
How HDAC3 Helps TR2 Get to PML
publication
Evidence: moderate
Author Information
Author(s): Pawan Gupta, Ping-Chih Ho, Sung Gil Ha, Yi-Wei Lin, Li-Na Wei
Primary Institution: University of Minnesota Medical School
Hypothesis
How is phosphorylated TR2 recruited to PML nuclear bodies?
Conclusion
HDAC3 acts as a carrier for phosphorylated TR2 to PML, independent of its deacetylase activity.
Supporting Evidence
- HDAC3 interacts with TR2 and enhances its recruitment to PML.
- The carrier function of HDAC3 is independent of its deacetylase activity.
- Phosphorylation of TR2 at Thr-210 is crucial for its interaction with HDAC3.
Takeaway
This study shows that a protein called HDAC3 helps another protein, TR2, move to a specific part of the cell called PML, which is important for its function.
Methodology
The study used in vitro and in vivo systems to investigate the interaction between HDAC3 and TR2.
Statistical Information
P-Value
p<0.01
Statistical Significance
p<0.01
Digital Object Identifier (DOI)
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