A Syd-1 homologue regulates pre- and postsynaptic maturation in Drosophila
| Autor: | Jorg Körner, Sara Mertel, Henning Urlaub, David Owald, Frauke Christiansen, Manuela Schmidt, Christina Zube, Stephan J. Sigrist, Christine Quentin, Harald Depner, Carolin Wichmann, Karl Mechtler, Wernher Fouquet |
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| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Proteomics
Embryo Nonmammalian Longevity Neuromuscular Junction Presynaptic Terminals Plasma protein binding Biology Neuromuscular junction Article chemistry.chemical_compound Postsynaptic potential medicine Animals Drosophila Proteins Neurotransmitter Receptor Research Articles Sequence Homology Amino Acid GTPase-Activating Proteins Glutamate receptor Synapsis Intracellular Signaling Peptides and Proteins Cell Biology Synaptic Potentials Phosphoproteins Transport protein Cell biology Protein Transport medicine.anatomical_structure Drosophila melanogaster Phenotype chemistry Receptors Glutamate Mutation Locomotion Protein Binding |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | A proteomics approach identifies Drosophila Syd-1 as a Bruchpilot binding partner that controls maturation on both sides of the neuromuscular junction. Active zones (AZs) are presynaptic membrane domains mediating synaptic vesicle fusion opposite postsynaptic densities (PSDs). At the Drosophila neuromuscular junction, the ELKS family member Bruchpilot (BRP) is essential for dense body formation and functional maturation of AZs. Using a proteomics approach, we identified Drosophila Syd-1 (DSyd-1) as a BRP binding partner. In vivo imaging shows that DSyd-1 arrives early at nascent AZs together with DLiprin-α, and both proteins localize to the AZ edge as the AZ matures. Mutants in dsyd-1 form smaller terminals with fewer release sites, and release less neurotransmitter. The remaining AZs are often large and misshapen, and ectopic, electron-dense accumulations of BRP form in boutons and axons. Furthermore, glutamate receptor content at PSDs increases because of excessive DGluRIIA accumulation. The AZ protein DSyd-1 is needed to properly localize DLiprin-α at AZs, and seems to control effective nucleation of newly forming AZs together with DLiprin-α. DSyd-1 also organizes trans-synaptic signaling to control maturation of PSD composition independently of DLiprin-α. |
| Databáze: | OpenAIRE |
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