Abstract
Abl is an axonal tyrosine kinase that has yet to be clearly linked to a receptor; Notch is a receptor for which the signaling pathway remains incompletely understood. We show here that Notch and abl mutations interact synergistically to produce synthetic lethality and defects in axon extension. Surprisingly, we cannot account for these axonal aberrations on the basis of changes in cell identity. We show, moreover, that Notch is present in the growth cones of extending axons, and that the Abl accessory protein Disabled binds to a signaling domain of Notch in vitro. We therefore speculate that Disabled and Abl may play a role in Notch signaling in Drosophila axons, perhaps by binding to the Notch intracellular domain.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Axons / physiology*
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Cells, Cultured
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Cloning, Molecular
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Drosophila / embryology*
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Drosophila Proteins*
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Embryo, Nonmammalian / physiology*
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Genes, Insect
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Genes, Lethal
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Membrane Proteins / physiology*
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Models, Biological
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Muscles / embryology
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Nerve Tissue Proteins / metabolism
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Nervous System / embryology*
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Neurons / physiology*
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Protein Biosynthesis
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins c-abl / genetics
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Proto-Oncogene Proteins c-abl / metabolism*
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Receptors, Cell Surface / physiology*
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Receptors, Notch
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Recombinant Proteins / metabolism
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Signal Transduction / physiology*
Substances
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Drosophila Proteins
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Membrane Proteins
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N protein, Drosophila
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Nerve Tissue Proteins
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Receptors, Cell Surface
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Receptors, Notch
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Recombinant Proteins
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dab protein, Drosophila
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Protein-Tyrosine Kinases
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Proto-Oncogene Proteins c-abl