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Elife. 2019 Feb 4;8. pii: e42690. doi: 10.7554/eLife.42690.

Transsynaptic interactions between IgSF proteins DIP-α and Dpr10 are required for motor neuron targeting specificity.

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Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, United States.
Graduate Program in Cell and Molecular Biology, University of Chicago, Chicago, United States.
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.
Department of Biological Chemistry, University of California, Los Angeles, Los Angeles, United States.
Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.


The Drosophila larval neuromuscular system provides an ideal context in which to study synaptic partner choice, because it contains a small number of pre- and postsynaptic cells connected in an invariant pattern. The discovery of interactions between two subfamilies of IgSF cell surface proteins, the Dprs and the DIPs, provided new candidates for cellular labels controlling synaptic specificity. Here we show that DIP-α is expressed by two identified motor neurons, while its binding partner Dpr10 is expressed by postsynaptic muscle targets. Removal of either DIP-α or Dpr10 results in loss of specific axonal branches and NMJs formed by one motor neuron, MNISN-1s, while other branches of the MNISN-1s axon develop normally. The temporal and spatial expression pattern of dpr10 correlates with muscle innervation by MNISN-1s during embryonic development. We propose a model whereby DIP-α and Dpr10 on opposing synaptic partners interact with each other to generate proper motor neuron connectivity.


Cell-surface proteins; D. melanogaster; IgSF; cell biology; muscle innervation; neuromuscular circuit; neuroscience; synaptic connectivity

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