Abstract
Tripartite (three-part) synapses are defined by physical and functional interactions of glia with pre- and post-synaptic elements. Although tripartite synapses are thought to be of widespread importance in neurological health and disease, we are only beginning to develop an understanding of glial contributions to synaptic function. In contrast to studies of neuronal mechanisms, a significant limitation has been the lack of an invertebrate genetic model system in which conserved mechanisms of tripartite synapse function may be examined through large-scale application of forward genetics and genome-wide genetic tools. Here we report a Drosophila tripartite synapse model which exhibits morphological and functional properties similar to those of mammalian synapses, including glial regulation of extracellular glutamate, synaptically-induced glial calcium transients and glial coupling of synapses with tracheal structures mediating gas exchange. In combination with classical and cell-type specific genetic approaches in Drosophila, this model is expected to provide new insights into the molecular and cellular mechanisms of tripartite synapse function.
Highlights
Previous studies have revealed important roles for glia in synapse development and function as well as neurological disorders including Amyotropic Lateral Sclerosis (ALS), Epilepsy, Huntington’s Disease and drug abuse
Presynaptic boutons of Dorsal Longitudinal Muscle (DLM) neuromuscular synapses are enveloped by glial processes. This may be visualized through immunofluorescence of the endogenous glialspecific glutamate transporter, dEAAT1 (Figure 1A–C and [18]) and by ultrastructural analysis showing that glial processes cover the bouton surface which is not in contact with the muscle (Figure 1D)
Encapsulation of synapses by glia has been described in detail for mammalian glutamatergic synapses such as the cerebellar climbing fiber (CF) to Purkinje Cell (PC) synapse [22]
Summary
Previous studies have revealed important roles for glia in synapse development and function as well as neurological disorders including Amyotropic Lateral Sclerosis (ALS), Epilepsy, Huntington’s Disease and drug abuse (reviewed in [1,2,3,4,5,6,7,8,9]). Despite this progress, new and complementary approaches are needed to further define the molecular mechanisms of tripartite synapse function. We have extended our studies of adult DLM neuromuscular synapses to establish a tripartite synapse model exhibiting conserved morphological and functional properties with respect to mammalian tripartite synapses
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