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A more recent version of this article appeared on April 1, 2004
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Submitted on May 27, 2003
Revised on October 13, 2003
Accepted on December 19, 2003
1 Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA, The first two authors contributed equally to this work
2 Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA, Instituto de Neurociencias CSIC-UMH, Universidad Miguel Hernandez, San Juan de Alicante, 03550 Spain, The first two authors contributed equally to this work
3 Instituto de Neurociencias CSIC-UMH, Universidad Miguel Hernandez, San Juan de Alicante, 03550 Spain, MRC Center for Developmental Neurobiology, King’s College, London SE1 1UL, UK
4 Instituto de Neurociencias CSIC-UMH, Universidad Miguel Hernandez, San Juan de Alicante, 03550 Spain
5 Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA
* Corresponding author. E-mail address: hortsch{at}umich.edu.
Neural cell adhesion molecules (CAMs) are important players during neurogenesis, neurite outgrowth, as well as axonal fasciculation and pathfinding. Some of these developmental processes entail the activation of cellular signaling cascades. Pharmacological and genetic evidence indicates that the neurite outgrowth-promoting activity of L1-type CAMs is at least in part mediated by the stimulation of neuronal receptor tyrosine kinases (RTKs), especially FGF and EGF receptors. It has long been suspected that neural CAMs might physically interact with RTKs, but their activation by specific cell adhesion events has not been directly demonstrated. Here we report that gain-of-function conditions of the Drosophila L1-type CAM Neuroglian result in profound sensory axon pathfinding defects in the developing Drosophila wing. This phenotype can be suppressed by decreasing the normal gene dosage of the Drosophila EGF receptor gene. Furthermore, in Drosophila S2 cells, cell adhesion mediated by human L1-CAM results in the specific activation of EGF tyrosine kinase at cell contact sites and EGF receptors engage in a physical interaction with L1-CAM molecules. Thus L1-type CAMs are able to promote the adhesion-dependent activation of EGF receptor signaling in vitro and in vivo.
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