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.

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.

Association of curvature generating proteins to the Golgi membranes by sphingomyelin metabolism essentially controls the flatness of a Golgi cisterna that is necessary for efficient sorting and export.

The phosphorylation of FLS2 may activate flg22-triggered immunity by facilitating the partitioning of FLS2 into functional AtRem1.3-associated nanodomains.

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.

The local PI(4,5)P₂ nanodomain promotes the dimerization and activation of EGFR in the plasma membrane, whereas activated EGFR dissolves the nanodomain structure of PI(4,5)P₂ through PLCγ.

Small probes show that most AMPA receptors are constrained near or in the synapses.

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

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

Ca²⁺ channels and release sensors at a fast central synapse are tightly coupled, which minimizes the effect of extracellular Ca²⁺ concentration on the timing of transmitter release.