Neurexins are a family of neuron-specific cell surface proteins that contain hundreds of isoforms. These isoforms are generated from two different promoters in three different genes that code for many splice-variant transcripts. In rat, neurexins include 160-200 kDa α-neurexins and 90-100 kDa β-neurexins, which include multipe isoforms identified as neurexin I, II, or III. Full-length α-neurexins contain three repeating domains that include a left arm (A) cell interaction module (LNS), a central EGF domain, and a right arm (B) LNS. β-neurexins are identical to α-neurexins in the C-terminal region, but lack the five LNS repeats and three EGF domains of α -neurexins. Neurexin Iα was first characterized as a Ca2+-dependent receptor for α-latrotoxin, the excitatory neurotoxin in black widow spider venom. The C-terminus of Neurexin Iα interacts with the synaptic vesicle protein, synaptotagmin, while the three repeated sequences in the extracellular region have homology to cell adhesion-related proteins. Thus, Neurexin Iα may be important for cell-cell interactions and synaptic protein localization during the neuronal differentiation.
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