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Related Experiment Video

Updated: Dec 26, 2025

Dissection and Imaging of Active Zones in the Drosophila Neuromuscular Junction
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Drosophila enabled promotes synapse morphogenesis and regulates active zone form and function.

Elizabeth M McNeill1, Cheryl Thompson2, Brett Berke3

  • 1Department of Food Science and Human Nutrition, Iowa State University, Ames, IA, USA. emcneill@iastate.edu.

Neural Development
|March 19, 2020
PubMed
Summary
This summary is machine-generated.

Enabled (Ena) protein is crucial for presynaptic terminal development and function, regulating bouton formation and neurotransmission. This study reveals Ena

Keywords:
ActinDrosophilaEna/VASP, DlarReceptor protein tyrosine phosphataseSynapse

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Developmental Biology

Background:

  • The actin cytoskeleton is vital for synapse development, neurotransmission, and plasticity.
  • Enabled (Ena), an actin-associated protein, influences Drosophila neuromuscular junction development postsynaptically.
  • Presynaptic roles and regulation of Ena remain largely unknown.

Purpose of the Study:

  • To investigate the presynaptic functions of Ena in neuronal morphology and ultrastructure.
  • To elucidate the regulatory pathway involving Ena at the presynaptic terminal.

Main Methods:

  • Conditional genetic manipulation in Drosophila.
  • Epistasis experiments to determine pathway interactions.

Main Results:

  • Presynaptic Ena promotes bouton and branch morphogenesis, contrasting its postsynaptic inhibitory role.
  • Presynaptic Ena functions downstream of the Dlar receptor tyrosine phosphatase pathway.
  • Ena regulates presynaptic varicosity addition, active zone size, synaptic vesicle recruitment, and spontaneous glutamate release.

Conclusions:

  • Ena is essential for presynaptic terminal morphogenesis and bouton addition, controlled by the Dlar pathway.
  • Ena influences active zone structure and neurotransmission.
  • Ena integrates multiple pathways governing synapse form and function, unlike Dlar.