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doi: 10.1242/10.1242/dev.00545

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Interactions between the secreted protein Amalgam, its transmembrane receptor Neurotactin and the Abelson tyrosine kinase affect axon pathfinding

Eric C. Liebl^1,, R. Grant Rowe¹, David J. Forsthoefel², Amanda L. Stammler¹, Erica R. Schmidt^1,*, Michelle Turski^2, and Mark A. Seeger²

¹ Department of Biology, Denison University, Granville, OH 43023, USA
² Department of Molecular Genetics and The Center for Molecular Neurobiology, The Ohio State University, Columbus, OH 43210, USA
^* Present address: College of Medicine, The Ohio State University, Columbus, OH 43210, USA
Present address: University Program in Genetics, Duke University, Durham, NC 27708, USA

Author for correspondence (e-mail: liebl{at}denison.edu)

Accepted 14 April 2003

Two novel dosage-sensitive modifiers of the Abelson tyrosine kinase (Abl) mutant phenotype have been identified. Amalgam (Ama) is a secreted protein that interacts with the transmembrane protein Neurotactin (Nrt) to promote cell:cell adhesion. We have identified an unusual missense ama allele, ama^M109, which dominantly enhances the Abl mutant phenotype, affecting axon pathfinding. Heterozygous null alleles of ama do not show this dominant enhancement, but animals homozygous mutant for both ama and Abl show abnormal axon outgrowth. Cell culture experiments demonstrate the Ama^M109 mutant protein binds to Nrt, but is defective in mediating Ama/Nrt cell adhesion. Heterozygous null alleles of nrt dominantly enhance the Abl mutant phenotype, also affecting axon pathfinding. Furthermore, we have found that all five mutations originally attributed to disabled are in fact alleles of nrt. These results suggest Ama/Nrt-mediated adhesion may be part of signaling networks involving the Abl tyrosine kinase in the growth cone.

Key words: Neural development, Axon pathfinding, Abelson tyrosine kinase, Abl, amalgam, disabled, neurotactin, Drosophila melanogaster

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