Ubiquitination of K-Ras enhances activation and facilitates binding to select downstream effectors.
Sci Signal. 2011; 4(163):ra13
Sasaki AT, Carracedo A, Locasale JW, Anastasiou D, ..., Haviv S, Asara JM, Pandolfi PP, Cantley LC. Sasaki AT, Carracedo A, Locasale JW, Anastasiou D, Takeuchi K, Kahoud ER, Haviv S, Asara JM, Pandolfi PP, Cantley LC. Sci Signal. 2011; 4(163):ra13
This study reveals the monoubiquitination of K-Ras as a novel regulatory mechanism controlling K-Ras' activity and signaling specificity.
The reversible post-translational modification of proteins, such as phosphorylation, acetylation and ubiquitination, is an efficient way of modulating protein function and increasing signaling...
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