Structurally and functionally unique complexins at retinal ribbon synapses |
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| Authors: | Reim Kerstin Wegmeyer Heike Brandstätter Johann Helmut Xue Mingshan Rosenmund Christian Dresbach Thomas Hofmann Kay Brose Nils |
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| Affiliation: | Department of Molecular Neurobiology, Max-Planck-Institute for Experimental Medicine, D-37075 G?ttingen, Germany. |
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| Abstract: | Ribbon synapses in retinal sensory neurons maintain large pools of readily releasable synaptic vesicles. This allows them to release several hundreds of vesicles per second at every presynaptic release site. The molecular components that cause this high transmitter release efficiency of ribbon synapses are unknown. In the present study, we identified and characterized two novel vertebrate complexins (CPXs), CPXs III and IV, that are the only CPX isoforms present in retinal ribbon synapses. CPXs III and IV are COOH-terminally farnesylated, and, like CPXs I and II, bind to SNAP receptor complexes. CPXs III and IV can functionally replace CPXs I and II, and their COOH-terminal farnesylation regulates their synaptic targeting and modulatory function in transmitter release. The novel CPXs III and IV may contribute to the unique release efficacy of retinal sensory neurons. |
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