A robust fluorescence microscopy-based data acquisition and analysis framework affords the precise measurement of cell surface receptor affinities toward their cognate ligands and their densities in live cells/tissues.
The modularity and unequivocal input/response of Notch signaling are harnessed to measure cell-surface shedding of diverse transmembrane receptors to identify new proteolytic switches and detect modulation of proteolysis by therapeutics.
Genetic and biochemical analyses demonstrate that cell-surface lectin receptors can potentially function as extracellular NAD+-binding receptors and provide direct evidence for extracellular NAD+ being a bona fide endogenous signaling molecule in plants.
Fly protein families Dprs and DIPs can create a multitude of complementary interfaces for homo- and heterophilic adhesion complexes, resulting in instructive roles for connectivity in the motor neuron circuitry.
β-adrenergic receptors at the Golgi apparatus activate a local signaling pathway, not accessed by cell surface receptors, to drive cardiac hypertrophy and could represent a target for heart failure therapy.