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

Cytosolic S100A8/A9 enhances Ca²⁺ availability at LFA-1 adhesion sites, facilitating neutrophil recruitment and extravasation by supporting proper integrin signaling and cytoskeletal rearrangement.

Nanodomain clustering of cAMP effectors represents a novel mechanism of cAMP compartmentation within an oscillatory signaling circuit.

Although genetically and biochemically linked, the plant immune and growth receptors FLS2 and BRI1 form dispersed receptor clusters within the plasma membrane that are spatiotemporally separated.

ICAM-1 engagement controls hepatic cell polarity, but this receptor can also signal without prior leukocyte interaction, thanks to its confinement into apical, microvilli-enriched, bile-canalicular domains and its actin connector EBP50.

Single-molecule localization imaging shows that the Nipah virus fusion protein forms nanoscale clusters on cell and viral membranes that favor membrane fusion activation.

Manipulating nanoscale spacing of Fcγ receptors using DNA origami demonstrates that ligand clustering regulates receptor phosphorylation and phagocytosis.

Mobile and immobile GABA_A receptors in the C. elegans neuromuscular synapse are stabilized by two distinct protein scaffolds.

This article reviews the latest studies that have used super-resolution microscopy and cluster analysis methodologies to study the mechanism of protein kinase signalling hubs and their organisation at nanoscale.

Super-resolution imaging reveals that the microtubule-associated protein Tau regulates the Fyn kinase organisation in dendrites, and that the frontotemporal dementia mutant Tau promotes aberrant Fyn clustering, potentially leading to synaptic dysfunction.