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The Journal of Neuroscience, July 23, 2003, 23(16):6567-6575

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N- and C-Terminal Domains of -Catenin, Respectively, Are Required to Initiate and Shape Axon Arbors of Retinal Ganglion Cells In Vivo

Tamira M. Elul,^1,2 Nikole E. Kimes,^1,2 Minoree Kohwi,¹ and Louis F. Reichardt^1,2

¹Department of Physiology, University of California San Francisco, and ²Howard Hughes Medical Institute, San Francisco, California 94143

We used deletion mutants to study -catenin function in axon arborization of retinal ganglion cells (RGCs) in live Xenopus laevis tadpoles. A deletion mutant catARM consists of the N- and C-terminal domains of wild-type -catenin that contain, respectively, -catenin and postsynaptic density-95 (PSD-95)/discs large (Dlg)/zona occludens-1 (ZO-1) (PDZ) binding sites but lacks the central armadillo repeat region that binds cadherins and other proteins. Expression of ARM in RGCs of live tadpoles perturbed axon arborization in two distinct ways: some RGC axons did not form arbors, whereas the remaining RGC axons formed arbors with abnormally long and tangled branches. Expression of the N- and C-terminal domains of -catenin separately in RGCs resulted in segregation of these two phenotypes. The axons of RGCs overexpressing the N-terminal domain of -catenin developed no or very few branches, whereas axons of RGCs overexpressing the C-terminal domain of -catenin formed arbors with long, tangled branches. Additional analysis revealed that the axons of RGCs that did not form arbors after overexpression of ARM or the N-terminal domain of -catenin were frequently mistargeted within the tectum. These results suggest that interactions of the N-terminal domain of -catenin with -catenin and of the C-terminal domain with PDZ domain-containing proteins are required, respectively, to initiate and shape axon arbors of RGCs in vivo.

Key words: -catenin; -catenin; PDZ proteins; lipofection; axon arborization; axon branching; retinal ganglion cells; Xenopus laevis

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Received Apr. 14, 2003; revised May. 23, 2003; accepted May. 23, 2003.

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