The Slit Receptor EVA-1 Coactivates a SAX-3/Robo–Mediated Guidance Signal in C. elegans

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Science  28 Sep 2007:
Vol. 317, Issue 5846, pp. 1934-1938
DOI: 10.1126/science.1144874

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The SAX-3/roundabout (Robo) receptor has Shiga-like toxin 1 (SLT-1)/Slit–dependent and –independent functions in guiding cell and axon migrations. We identified enhancer of ventral-axon guidance defects of unc-40 mutants (EVA-1) as a Caenorhabditis elegans transmembrane receptor for SLT-1. EVA-1 has two predicted galactose-binding ectodomains, acts cell-autonomously for SLT-1/Slit–dependent axon migration functions of SAX-3/Robo, binds to SLT-1 and SAX-3, colocalizes with SAX-3 on cells, and provides cell specificity to the activation of SAX-3 signaling by SLT-1. Double mutants of eva-1 or slt-1 with sax-3 mutations suggest that SAX-3 can (when slt-1 or eva-1 function is reduced) inhibit a parallel-acting guidance mechanism, which involves UNC-40/deleted in colorectal cancer.

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