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First published online April 22, 2009

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Regulating ribbon synapses

Ribbon synapses are specialised chemical synapses with a presynaptic plate-like organelle - the ribbon. Ribbons bind to a high number of synaptic vesicles and are anchored to the plasma membrane close to voltage-gated Ca²⁺ channels, which enables ribbon synapses to respond properly to changes in membrane potentials. Ca²⁺-triggered synaptic vesicle fusion involves SNARE proteins, which are regulated by other factors such as complexin (Cplx)-family proteins. On page 1352, Nils Brose and colleagues investigate for the first time the role of Cplx3 and Cplx4 in the structure and function of ribbon synapses in the mouse retina. Examination of Cplx3-, Cplx4- and Cplx3/4-knockout mice reveals that retinal anatomy and neuronal morphology is normal in these mice, but that ribbon synaptic structure is abnormal in Cplx3/4-knockout mice. In agreement with this result, double-knockout mice have a mild vision defect. Electroretinographic recordings show that the lack of either Cplx3 or Cplx4 causes limited abnormalities in photoreceptor function and synaptic transmission in the retina; however, the deletion of both genes has a cooperative effect and causes significant functional changes. The authors conclude that Cplx3 and Cplx4 are important for regulating transmitter release at retinal ribbon synapses.

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Aberrant function and structure of retinal ribbon synapses in the absence of complexin 3 and complexin 4

Kerstin Reim, Hanna Regus-Leidig, Josef Ammermüller, Ahmed El-Kordi, Konstantin Radyushkin, Hannelore Ehrenreich, Johann Helmut Brandstätter, and Nils Brose
JCS 2009 122: 1352-1361. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?