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.

The perception of endogenous RALF signaling peptides modulates the plasma membrane nanoscale organization of receptor kinases to regulate plant immune signaling.

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.

The dodecahelical membrane anchors of mammalian adenylyl cyclase isoforms are receptors for unsaturated free fatty acids and, as a tonic signal, enhance or attenuate GPCR/Gsα-stimulated cyclic AMP formation.

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

Atomistic simulations reveal how lipids can allosterically modulate membrane receptors.

A designer peptide inhibits the T cell receptor through allosteric binding to the transmembrane region.

The cell membrane receptors of juvenile hormone, CAD96CA and FGFR1, regulate the genomic effects of juvenile hormone by phosphorylating intracellular receptor.

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

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