Recent experiments have begun to decipher the molecular dialog that me
diates differentiation at sites of synaptic contact between neurons an
d their targets. It had been hypothesized that the protein agrin is re
leased by axon terminals at embryonic neuromuscular junctions and bind
s to a receptor on the myofiber surface to trigger postsynaptic differ
entiation. Now a genetic 'knockout' experiment has confirmed the essen
tial role of agrin in signaling between developing nerve and muscle((1
)). A second 'knockout' has shown that the muscle-specific receptor ty
rosine kinase MuSK is a critical element in the agrin-induced signalin
g cascade((2)). Additional results suggest that MuSK may comprise a po
rtion of the agrin receptor((3)).