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.

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

In silico modeling identify allosteric CXCR4 modulators that block receptor nanoclustering and chemoattractant sensing without affecting other CXCL12-mediated functions, and reduce tumorigenesis and metastasis in a zebrafish model.

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

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.

Advanced imaging methods reveal that Siglec-1 spatial distribution on mature dendritic cells is regulated by components of the actin polymerization machinery impacting on its engagement to HIV-particles and virus sequestration toward virus-containing compartments.

SNARE–SNARE interactions that have previously only been proposed to participate in membrane fusion on the nanoscale also serve to organize SNARE domains on the mesoscale.

Unprecedented resolution of the molecular mechanisms of plant membrane protein anchoring involving phospholipids and sterols reveals the control of spatio-temporal segregation into plasma membrane nanodomains.

Dopamine transporter (DAT) interaction with furopyrimidine called AIM-100 in intact cells leads to dramatic oligomerization, nanoclustering and endocytosis of DAT by a novel mechanism coupled to the transporter molecule conformation.