Both the C-Terminal Polylysine Region and the Farnesylation of K-RasB Are Important for Its Specific Interaction with Calmodulin
2011
K-RasB and Calmodulin Interaction Study
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Wu Ling-Jia, Xu Li-Rong, Chen Jun-Ming, Liang Jie, Yi
Primary Institution: State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China
Hypothesis
The C-terminal polylysine region and farnesylation of K-RasB are important for its specific interaction with calmodulin.
Conclusion
The study shows that both the polylysine region and farnesylation of K-RasB are crucial for its interaction with calmodulin.
Supporting Evidence
- K-RasB interacts with calmodulin in a GTP dependent manner.
- Farnesylation enhances the binding affinity of K-RasB to calmodulin.
- Mutations in the polybasic domain of K-RasB decrease its binding affinity to calmodulin.
- Calmodulin binding is specific to K-RasB and not to other Ras isoforms.
Takeaway
K-RasB needs certain parts to stick to calmodulin, which helps it work properly in cells.
Methodology
Fluorescence spectroscopy and isothermal titration calorimetry were used to study the interaction between K-RasB and calmodulin.
Statistical Information
P-Value
p<0.05
Digital Object Identifier (DOI)
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