Abstract

Large‐scale pruning, the developmentally regulated degeneration of axons or dendrites, is an important specificity mechanism during neuronal circuit formation. The peripheral sensory class IV dendritic arborization (c4da) neurons of Drosophila larvae specifically prune their dendrites at the onset of metamorphosis in an ecdysone‐dependent manner. Dendrite pruning requires local cytoskeleton remodeling, and the actin‐severing enzyme Mical is an important ecdysone target. In a screen for pruning factors, we identified the protein phosphatase 2 A (PP2A). PP2A interacts genetically with the actin‐severing enzymes Mical and cofilin as well as other actin regulators during pruning. Moreover, Drosophila cofilin undergoes a change in localization at the onset of metamorphosis indicative of a change in actin dynamics. This change is abolished both upon loss of Mical and PP2A. We conclude that PP2A regulates actin dynamics during dendrite pruning.

Highlights

  • Neurite pruning, the physiological degeneration of axons or dendrites during development, is an important specificity mechanism during neuronal circuit formation [1,2]

  • We identified an important role for the protein phosphatase phosphatase 2 A (PP2A) during large-scale dendrite pruning of Drosophila c4da neurons during metamorphosis

  • Our genetic interaction studies show that the pruning defects caused by loss of PP2A can be suppressed by overexpression of the actin-severing enzyme Mical

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Summary

Introduction

The physiological degeneration of axons or dendrites during development, is an important specificity mechanism during neuronal circuit formation [1,2]. The first morphological signs of dendrite pruning are seen at around 3–5 h after puparium formation (h APF), when dendrites start to show local thinnings and varicosities in their proximal regions that appear to be due to changes in cytoskeletal and membrane stability. At these proximal sites, the dendrites are eventually severed between 6 and 12 h APF. Once severed, pruned dendrites are subsequently fragmented in a caspase-dependent manner and phagocytosed by epidermal cells [16,17]

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