Self-avoidance alone does not explain the function of Dscam1 in mushroom body axonal wiring

Curr Biol. 2022 Jul 11;32(13):2908-2920.e4. doi: 10.1016/j.cub.2022.05.030. Epub 2022 Jun 2.

Abstract

Alternative splicing of Drosophila Dscam1 into 38,016 isoforms provides neurons with a unique molecular code for self-recognition and self-avoidance. A canonical model suggests that the homophilic binding of identical Dscam1 isoforms on the sister branches of mushroom body (MB) axons supports segregation with high fidelity, even when only a single isoform is expressed. Here, we generated a series of mutant flies with a single exon 4, 6, or 9 variant, encoding 1,584, 396, or 576 potential isoforms, respectively. Surprisingly, most of the mutants in the latter two groups exhibited obvious defects in the growth, branching, and segregation of MB axonal sister branches. This demonstrates that the repertoires of 396 and 576 Dscam1 isoforms were not sufficient for the normal patterning of axonal branches. Moreover, reducing Dscam1 levels largely reversed the defects caused by reduced isoform diversity, suggesting a functional link between Dscam1 expression levels and isoform diversity. Taken together, these results indicate that canonical self-avoidance alone does not explain the function of Dscam1 in MB axonal wiring.

Keywords: CRISPR-Cas9; Drosophila; Dscam; isoform diversity; mushroom body; neuronal wiring; self-avoidance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Axons / metabolism
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism
  • Drosophila / genetics
  • Drosophila / metabolism
  • Drosophila Proteins* / metabolism
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism
  • Mushroom Bodies* / metabolism
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism

Substances

  • Cell Adhesion Molecules
  • Drosophila Proteins
  • Protein Isoforms