Motorneurons require cysteine string protein-α to maintain the readily releasable vesicular pool and synaptic vesicle recycling.

Cysteine string protein-α (CSP-α) is a synaptic vesicle protein that prevents activity-dependent neurodegeneration by poorly understood mechanisms. We have studied the synaptic vesicle cycle at the motor nerve terminals of CSP-α knock-out mice expressing the synaptopHluorin transgene. Mutant nerve terminals fail to sustain prolonged release and the number of vesicles available to be released decreases.

Metabotropic actions of kainate receptors in dorsal root ganglion cells.

Kainate receptors are widely distributed in the CNS, but also in the PNS. Dorsal root ganglia are enriched in this subtype of glutamate ionotropic receptors. In addition to their activity as ligand-gated ion channels, kainate receptors exhibit other properties already characterized in other systems, such as hippocampus, i.

PKC-dependent autoregulation of membrane kainate receptors.

Agonists of kainate receptors (KARs) cause both the opening of the associated ion channels and the activation of signalling pathways driven by G-proteins and PKC. Here we report the existence of an unknown mechanism of KAR autoregulation, involving the interplay of this two signalling mechanisms. Repetitive activation of native KARs evoked the rundown of the ionotropic responses in a manner that was dependent on the activation of PKC.

Noncanonical signaling by ionotropic kainate receptors.

The potent neurotoxin kainate activates ion channel-forming receptors. However, it can also activate a G protein-coupled signaling pathway to inhibit transmitter release in central neurons. It remains unclear whether the same receptor complex is involved in both signaling activities.