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.

FERONIA receptor kinase interacts with phosphatidylinositol-anchored proteins LORELEI and LLG1 to ensure its proper functional location in the cell membrane and engages them as co-receptors on the cell surface to mediate a broad spectrum of growth and signaling processes.

The X-ray structure of the SAS-6 cartwheel hub from Leishmania major demonstrates that SAS-6 can be sufficient to determine centriolar cartwheel symmetry.

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

Elevating FUS level by saturating autoregulation loop in mice causes aggressive motor neuron disease via disrupting protein and RNA homeostasis.

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.

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.

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.

Dual FAK/PYK2 kinase inhibition disrupts GSK3β phosphorylation and may present a new treatment for colorectal cancer in patients carrying APC mutations.

Detailed structural analysis of NPAS1-ARNT and NPAS3-ARNT complexes, and further comparisons with other bHLH-PAS protein structures, show that this family of mammalian transcription factors have distinct ligand-binding pockets within their molecular architectures.