How Sumoylation Affects CoCoA's Role in Gene Regulation
Author Information
Author(s): Catherine K Yang, Jeong Hoon Kim, David K Ann, Michael R Stallcup
Primary Institution: University of Southern California
Hypothesis
Sumoylation differentially regulates the activities of the two activation domains of CoCoA.
Conclusion
Sumoylation of CoCoA differentially regulates its coactivator activity with nuclear receptors versus LEF1.
Supporting Evidence
- CoCoA is modified by SUMO1 at Lys-29, affecting its coactivator function.
- Sumoylation reduces the interaction between the N- and C-termini of CoCoA.
- The N-terminal activation domain is necessary for CoCoA's function with LEF1.
- The C-terminal activation domain is required for CoCoA's function with nuclear receptors.
- Fusion of SUMO1 to CoCoA enhances its activity with nuclear receptors.
- Sumoylation of CoCoA inhibits its activity with LEF1.
Takeaway
CoCoA is a helper protein that can change how it works based on a tiny tag called SUMO. This tag can make it better at helping some proteins but worse at helping others.
Methodology
The study involved in vitro and in vivo experiments to analyze the sumoylation of CoCoA and its effects on transcriptional activity.
Limitations
The study does not explore the potential external signals that might regulate the sumoylation of CoCoA.
Digital Object Identifier (DOI)
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