The CRMP protein has been extensively studied in mammals and has been implicated in control of neuronal growth cone dynamics. Originally identified as a mediator of semphorin repulsion signalling in cultured neurons (1), it has been shown by numerous studies to physically associate with a variety of intracellular signal transduction and cytoskeletal elements (2,3,4). However, the exact function of CRMP remains entirely unknown. In vertebrates, there are multiple CRMPs that are neuron-limited in their expression and that arise from a duplicated gene family. Our lab’s interest focuses upon using the powerful genetic capabilities of Drosophila to better understand how the CRMP protein functions in neurogenesis. The sole Drosophila CRMP protein is one of two proteins encoded by the crmp gene; the other protein, DHP, is the second enzymatic step of pyrimidine catabolism and apparently the ancestral protein in this protein family. These two proteins arise from differential splicing of the crmp primary transcript in non-neuronal and neuronal cells (5). At the protein sequence level, Drosophila CRMP and DHP are 91% identical, suggesting that the 9% divergent portion of the proteins accounts for the completely divergent functions of these proteins. Null, loss-of-function crmp mutations destroy DHP activity, but produce no developmental or distinct neurological phenotypes (6). Thus, we have turned to mis-expression of the CRMP and DHP proteins to detect gain-of-function phenotypes for these proteins and to further study their role in development.

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