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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sturgeon, Morgan Davis, Dustin Albers, Amanda Beatty, Derek Austin, Rik Ferguson, Matt Tounsel, Brittany Liebl, Faith L. W. |
| Description | Country affiliation: United States Author Affiliation: Sturgeon M ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Davis D ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Albers A ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Beatty D ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Austin R ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Ferguson M ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Tounsel B ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States.); Liebl FL ( Department of Biological Sciences, Southern Illinois University Edwardsville, Edwardsville, IL 62026, United States. Electronic address: fliebl@siue.edu.) |
| Abstract | The postsynaptic density (PSD) is a protein-rich network important for the localization of postsynaptic glutamate receptors (GluRs) and for signaling downstream of these receptors. Although hundreds of PSD proteins have been identified, many are functionally uncharacterized. We conducted a reverse genetic screen for mutations that affected GluR localization using Drosophila genes that encode homologs of mammalian PSD proteins. 42.8% of the mutants analyzed exhibited a significant change in GluR localization at the third instar larval neuromuscular junction (NMJ), a model synapse that expresses homologs of AMPA receptors. We identified the E3 ubiquitin ligase, Mib1, which promotes Notch signaling, as a regulator of synaptic GluR localization. Mib1 positively regulates the localization of the GluR subunits GluRIIA, GluRIIB, and GluRIIC. Mutations in mib1 and ubiquitous expression of Mib1 that lacks its ubiquitin ligase activity result in the loss of synaptic GluRIIA-containing receptors. In contrast, overexpression of Mib1 in all tissues increases postsynaptic levels of GluRIIA. Cellular levels of Mib1 are also important for the structure of the presynaptic motor neuron. While deficient Mib1 signaling leads to overgrowth of the NMJ, ubiquitous overexpression of Mib1 results in a reduction in the number of presynaptic motor neuron boutons and branches. These synaptic changes may be secondary to attenuated glutamate release from the presynaptic motor neuron in mib1 mutants as mib1 mutants exhibit significant reductions in the vesicle-associated protein cysteine string protein and in the frequency of spontaneous neurotransmission. |
| File Format | HTM / HTML |
| ISSN | 10447431 |
| Volume Number | 70 |
| e-ISSN | 10959327 |
| Journal | Molecular and Cellular Neuroscience |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-01-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Cell Biology Discipline Molecular Biology Discipline Neurology Drosophila Proteins Metabolism Motor Neurons Mutation Post-synaptic Density Receptors, Glutamate Synapses Ubiquitin-protein Ligases Animals Genetics Drosophila Melanogaster Neuromuscular Junction Signal Transduction Synaptic Transmission Physiology Journal Article Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Cellular and Molecular Neuroscience |
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