Structurally and functionally unique complexins at retinal ribbon synapses

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 synap...

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Bibliographic Details
Published in:The Journal of cell biology 2005-05, Vol.169 (4), p.669-680
Main Authors: Reim, Kerstin, Wegmeyer, Heike, Brandstätter, Johann Helmut, Xue, Mingshan, Rosenmund, Christian, Dresbach, Thomas, Hofmann, Kay, Brose, Nils
Format: Article
Language:English
Subjects:
Adaptor Proteins, Vesicular Transport
Amacrine cells
Animals
Cell Line
Cell membranes
Cellular biology
Complementary DNA
Eye Proteins - genetics
Eye Proteins - isolation & purification
Eye Proteins - metabolism
HEK293 cells
Humans
Membrane Proteins - genetics
Membrane Proteins - isolation & purification
Membrane Proteins - metabolism
Messenger RNA
Mice
Molecular Sequence Data
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - isolation & purification
Nerve Tissue Proteins - metabolism
Neurons
Organelles - metabolism
Photoreceptor Cells - metabolism
Photoreceptors
Protein Binding - physiology
Protein isoforms
Protein Prenylation - physiology
Protein Structure, Tertiary - physiology
Retina
Retina - metabolism
Sequence Homology, Amino Acid
Sequence Homology, Nucleic Acid
SNARE Proteins
Synapses
Synapses - metabolism
Synaptic Transmission - physiology
Vesicular Transport Proteins - metabolism
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200502115