Topic: presynaptic boutons

Understanding how neurons regulate their protein composition to refine synaptic connections across millimeters of space provides critical insights into the mechanisms of synaptic plasticity. The discovery of local protein synthesis in subcellular compartments has shown how neuronal activity can locally meet the metabolic demands of synaptic plasticity$^{1,2}$. Despite the experimental challenges posed by the long and complex branches of axons, the presence of mRNA and local protein synthesis in presynaptic boutons has been clearly demonstrated$^{3,5}$. In this study, we developed an in silico

The interplay of the calcium concentration and the anatomical structure at the presynaptic zone of presynaptic boutons is an important challenge of the relationship of form and function in (computational) neuroscience. A simple model system to study such basic effects is the neuromuscular junction of the Drosophila larva (NMJ). At this synapse, specific structures can be found. Its presynaptic boutons are larger than usual vertebrate synapses, also they bear several presynaptic zones. Different anatomic structures can be found at these zones. In part, they incorporate a so-called T-Bar, which,

Introduction: Neurotrypsin (NT) is a neuronal trypsin-like serine protease whose mutations cause severe mental retardation in humans. NT is activated in vitro by Hebbian-like conjunction of pre- and postsynaptic activities, which promote the formation of dendritic filopodia via proteolytic cleavage of the proteoglycan agrin. Aims: 1) to examine the functional importance of NT for synaptic plasticity, learning, and extinction of memory in juvenile and matured mice, and 2) to evaluate the therapeutic potential of an NT-generated fragment of agrin, agrin-22. Methods: 1-month-old “Juvenile” NT−/−