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.

A canonical class III adenylate cyclase with a membrane anchor of six transmembrane spans is regulated by a receptor of similar design, the quorum-sensing receptor from Vibrio harveyi.

Atomistic simulations reveal how lipids can allosterically modulate membrane receptors.

Functional reconstitution of a mammalian P2X7 receptor uncovers an intrinsic and lipid-dependent dye-permeable membrane pore.

Filamin, by recruiting a signaling complex to the postsynapse, orchestrates the correct formation and growth of postsynaptic membranes and localization of glutamate receptor subunits.

The mechanism of signaling receptor delivery to primary cilia involves a specific cellular role of a Rab protein that is critical for vertebrate development.

Single molecule microscopy combined with biochemical analyses show that a two-step lipid-binding mechanism of the SRP receptor balances the trade-off between speed and specificity during co-translational protein targeting.

Two receptors have been identified that can be targeted in melanocytes with selective small molecule agonists to modulate human skin color.

Membrane receptor proteins move through primary cilia largely by passive diffusion rather than by active intraflagellar transport.

Clustering the B cell receptor generates a membrane domain analogous to the liquid-ordered phase, localizing proteins involved in early receptor activation.