Proteolytic processing of Slit Authored: Garapati, P V, 2008-09-05 06:02:05 EC Number: 3.4 Edited: Garapati, P V, 2008-09-05 06:02:05 Pubmed10102266 Pubmed10102268 Reactome Database ID Release 43376149 Reactome, http://www.reactome.org ReactomeREACT_19284 Reviewed: Kidd, T, 2009-08-18 The full length Slit proteins are membrane bound via the extracellular matrix proteins when not bound to Robo receptors. These full length Slits undergo post translational modification and proteolytic processing to generate an N terminal fragment (Slit2 N) and a corresponding C terminal fragment (Slit2 C). Slit 2 is cleaved within the EGF repeats, between EGF5 and EGF6, by unknown proteases. Cleavage of Slit proteins is evolutionarily conserved, although the molecular biological significance is unknown. The N-terminal fragment of Slit2 stimulates growth and branching of dorsal root ganglia (DRG) axons, and this activity is opposed by un-cleaved Slit. The stimulation of axon branching is mediated by Robo receptors. Additional functional differences between the full-length and N-terminal forms have been discovered in their abilities to repel different populations of axons and dendrites. Finally, Slit can attract migrating muscles in the fly, and also human endothelial cells, both via Robo receptors.