Interactions between the Ig-Superfamily Proteins DIP-α and Dpr6/10 Regulate Assembly of Neural Circuits

Neuron
Shuwa XuS Lawrence Zipursky

Abstract

Drosophila Dpr (21 paralogs) and DIP proteins (11 paralogs) are cell recognition molecules of the immunoglobulin superfamily (IgSF) that form a complex protein interaction network. DIP and Dpr proteins are expressed in a synaptic layer-specific fashion in the visual system. How interactions between these proteins regulate layer-specific synaptic circuitry is not known. Here we establish that DIP-α and its interacting partners Dpr6 and Dpr10 regulate multiple processes, including arborization within layers, synapse number, layer specificity, and cell survival. We demonstrate that heterophilic binding between Dpr6/10 and DIP-α and homophilic binding between DIP-α proteins promote interactions between processes in vivo. Knockin mutants disrupting the DIP/Dpr binding interface reveal a role for these proteins during normal development, while ectopic expression studies support an instructive role for interactions between DIPs and Dprs in circuit development. These studies support an important role for the DIP/Dpr protein interaction network in regulating cell-type-specific connectivity patterns.

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Citations

May 3, 2020·Nature Communications·Alina P SergeevaBarry Honig
Aug 28, 2020·Frontiers in Neural Circuits·Aline Giselle Rangel OlguinArjun Krishnaswamy
Nov 5, 2020·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·P Robin Hiesinger
May 4, 2020·Cell·Joshua R Sanes, S Lawrence Zipursky
Aug 22, 2020·Current Opinion in Neurobiology·Joelle M Dorskind, Alex L Kolodkin
Jun 30, 2021·Proceedings of the National Academy of Sciences of the United States of America·Jennifer Malin, Claude Desplan

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