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Abstract
Extending axons in the developing nervous system are guided in part by repulsive cues.
Genetic analysis in Drosophila, reported in a companion to this paper, identifies
the Slit protein as a candidate ligand for the repulsive guidance receptor Roundabout
(Robo). Here we describe the characterization of three mammalian Slit homologs and
show that the Drosophila Slit protein and at least one of the mammalian Slit proteins,
Slit2, are proteolytically processed and show specific, high-affinity binding to Robo
proteins. Furthermore, recombinant Slit2 can repel embryonic spinal motor axons in
cell culture. These results support the hypothesis that Slit proteins have an evolutionarily
conserved role in axon guidance as repulsive ligands for Robo receptors.