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An in-depth binding profile analysis of BRAF domains related to RAF activation and autoinhibition unveils the distinctive roles of each domain in selecting preferred RAS isoforms and facilitating autoinhibition.

Cancer cells driven by mutations in KRAS or EGFR are dependent on DUSP6 to prevent ERK-induced cell death, creating a novel vulnerability for targeted therapy.

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

Deep mutagenesis experiments demonstrate that while cancer-causing mutations in Ras selectively alter regulatory interactions with GTPase-activating proteins, Ras is also activated by many mutations that decrease protein stability.

The nanoscopic landscape of the membrane has a direct impact on the spatiotemporal, and likely also the signaling, dynamics of Ras proteins.

The Ras activator RasGRP1 that impacts Ras signals in immune cells, leukemias, and colorectal cancer, switches to an active conformation aided by a pH-sensitive histidine residue in a central location of the RasGRP1 molecule.

Cancer-associated changes in small nucleolar RNAs and site-specific pseudouridine modifications impact ribosome activity.

Neuroligin 1 is a critical adhesion molecule which organizes AMPA receptor nanodomains in close vicinity to pre-synaptic release sites, and whose genetic or chemical disruption severely impairs synaptic transmission properties.

ELYS, a multifunctional protein with critical roles in the cell cycle, is essential for the vigorous proliferation and survival of difficult-to-treat cancers carrying mutations in the KRAS oncogene, making it a compelling target for novel drug treatments.

Non-invasive imaging of hippocampal neurodegeneration and structural reorganization during epileptogenesis allows the prediction of disease severity in mesial temporal lobe epilepsy, which may facilitate the early pharmacological intervention before seizure onset.