A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.

Proteomics and functional genomics coupled to an antibody discovery pipeline revealed the influence of oncogenic RAS signaling on the cell-surface proteome and resulted in the discovery of potential therapeutic targets for RAS-driven cancers.

Rare mutations in the switch III region of Ras can increase its nanoscale clustering, which enhances effector recruitment and downstream signaling.

The probability of a cellular response to a differentiation inducing signal is correlated with the dynamic expression of a Ras protein, and produces a ‘salt and pepper’ pattern of cell differentiation.

Small RNAs of distantly related plant pathogens, such as fungi and oomycetes, hijack the plant RNA-induced silencing complex to favor host infection.

A biosensor resource has been developed to monitor the intracellular interactions of RAS family proteins with effector molecules and the effects of inhibitors as an aid to drug development.

Two cell-penetrating peptides that inhibit Ras-ERK signalling and a potent clinically relevant MEK inhibitor block cocaine conditioned place preference and accelerate extinction of cocaine self-administration upon a single administration in mice.

A systems level reconstitution of H-Ras GTPase signaling reveals a rich space of tunable dynamic outputs and clarifies the consequences of oncogenic perturbations to signaling.

Palmitate turnover is controlled by distinct enzyme families with different specificities.