larval motor patterning relies on regulated alternative splicing of .

Recent studies capitalizing on the newly complete nanometer-resolution larval connectome have made significant advances in identifying the structural basis of motor patterning. However, the molecular mechanisms utilized by neurons to wire these circuits remain poorly understood. In this study we explore how cell-specific expression of two isoforms, which mediate isoform-specific homophilic binding, contributes to motor patterning and output of larvae.

Dscam2 suppresses synaptic strength through a PI3K-dependent endosomal pathway.

Dscam2 is a cell surface protein required for neuronal development in Drosophila; it can promote neural wiring through homophilic recognition that leads to either adhesion or repulsion between neurites. Here, we report that Dscam2 also plays a post-developmental role in suppressing synaptic strength. This function is dependent on one of two distinct extracellular isoforms of the protein and is autonomous to motor neurons.

Regulated Alternative Splicing of Is Necessary for Attaining the Appropriate Number of Photoreceptor Synapses.

How the brain makes trillions of synaptic connections using a genome of only 20,000 genes is a major question in modern neuroscience. Alternative splicing is one mechanism that can increase the number of proteins produced by each gene, but its role in regulating synapse formation is poorly understood. In , photoreceptors form a synapse with multiple postsynaptic elements including lamina neurons L1 and L2.