@article{TEXTUAL,
      recid = {9915},
      author = {Cheng, Shouqiang and Ashley, James and Kurleto, Justyna D.  and Lobb-Rabe, Meike and Park, Yeonhee Jenny and Carrillo,  Robert A. and Özkan, Engin},
      title = {Molecular basis of synaptic specificity by immunoglobulin  superfamily receptors in drosophila},
      journal = {eLife},
      address = {2019-01-28},
      number = {TEXTUAL},
      abstract = {In stereotyped neuronal networks, synaptic connectivity is  dictated by cell surface proteins, which assign unique  identities to neurons, and physically mediate axon guidance  and synapse targeting. We recently identified two groups of  immunoglobulin superfamily proteins in Drosophila, Dprs and  DIPs, as strong candidates for synapse targeting functions.  Here, we uncover the molecular basis of specificity in  Dpr–DIP mediated cellular adhesions and neuronal  connectivity. First, we present five crystal structures of  Dpr–DIP and DIP–DIP complexes, highlighting the  evolutionary and structural origins of diversification in  Dpr and DIP proteins and their interactions. We further  show that structures can be used to rationally engineer  receptors with novel specificities or modified affinities,  which can be used to study specific circuits that require  Dpr–DIP interactions to help establish connectivity. We  investigate one pair, engineered Dpr10 and DIP-α, for  function in the neuromuscular circuit in flies, and reveal  roles for homophilic and heterophilic binding in wiring.},
      url = {http://knowledge.uchicago.edu/record/9915},
}