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Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses
Complexin (Cplx) proteins modulate the core SNARE complex to regulate exocytosis. To understand the contributions of Cplx to signaling in a well-characterized neural circuit, we investigated how Cplx3, a retina-specific paralog, shapes transmission at rod bipolar (RB) → AII amacrine cell synapses in...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5134263/ https://www.ncbi.nlm.nih.gov/pubmed/27239031 http://dx.doi.org/10.1016/j.celrep.2016.05.012 |
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author | Mortensen, Lena S. Park, Silvia J.H. Ke, Jiang-bin Cooper, Benjamin H. Zhang, Lei Imig, Cordelia Löwel, Siegrid Reim, Kerstin Brose, Nils Demb, Jonathan B. Rhee, Jeong-Seop Singer, Joshua H. |
author_facet | Mortensen, Lena S. Park, Silvia J.H. Ke, Jiang-bin Cooper, Benjamin H. Zhang, Lei Imig, Cordelia Löwel, Siegrid Reim, Kerstin Brose, Nils Demb, Jonathan B. Rhee, Jeong-Seop Singer, Joshua H. |
author_sort | Mortensen, Lena S. |
collection | PubMed |
description | Complexin (Cplx) proteins modulate the core SNARE complex to regulate exocytosis. To understand the contributions of Cplx to signaling in a well-characterized neural circuit, we investigated how Cplx3, a retina-specific paralog, shapes transmission at rod bipolar (RB) → AII amacrine cell synapses in the mouse retina. Knockout of Cplx3 strongly attenuated fast, phasic Ca(2+)-dependent transmission, dependent on local [Ca(2+)] nanodomains, but enhanced slower Ca(2+)-dependent transmission, dependent on global intraterminal [Ca(2+)] ([Ca(2+)](I)). Surprisingly, coordinated multivesicular release persisted at Cplx3(−/−) synapses, although its onset was slowed. Light-dependent signaling at Cplx3(−/−) RB → AII synapses was sluggish, owing largely to increased asynchronous release at light offset. Consequently, propagation of RB output to retinal ganglion cells was suppressed dramatically. Our study links Cplx3 expression with synapse and circuit function in a specific retinal pathway and reveals a role for asynchronous release in circuit gain control. |
format | Online Article Text |
id | pubmed-5134263 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
record_format | MEDLINE/PubMed |
spelling | pubmed-51342632016-12-02 Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses Mortensen, Lena S. Park, Silvia J.H. Ke, Jiang-bin Cooper, Benjamin H. Zhang, Lei Imig, Cordelia Löwel, Siegrid Reim, Kerstin Brose, Nils Demb, Jonathan B. Rhee, Jeong-Seop Singer, Joshua H. Cell Rep Article Complexin (Cplx) proteins modulate the core SNARE complex to regulate exocytosis. To understand the contributions of Cplx to signaling in a well-characterized neural circuit, we investigated how Cplx3, a retina-specific paralog, shapes transmission at rod bipolar (RB) → AII amacrine cell synapses in the mouse retina. Knockout of Cplx3 strongly attenuated fast, phasic Ca(2+)-dependent transmission, dependent on local [Ca(2+)] nanodomains, but enhanced slower Ca(2+)-dependent transmission, dependent on global intraterminal [Ca(2+)] ([Ca(2+)](I)). Surprisingly, coordinated multivesicular release persisted at Cplx3(−/−) synapses, although its onset was slowed. Light-dependent signaling at Cplx3(−/−) RB → AII synapses was sluggish, owing largely to increased asynchronous release at light offset. Consequently, propagation of RB output to retinal ganglion cells was suppressed dramatically. Our study links Cplx3 expression with synapse and circuit function in a specific retinal pathway and reveals a role for asynchronous release in circuit gain control. 2016-05-26 2016-06-07 /pmc/articles/PMC5134263/ /pubmed/27239031 http://dx.doi.org/10.1016/j.celrep.2016.05.012 Text en This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Mortensen, Lena S. Park, Silvia J.H. Ke, Jiang-bin Cooper, Benjamin H. Zhang, Lei Imig, Cordelia Löwel, Siegrid Reim, Kerstin Brose, Nils Demb, Jonathan B. Rhee, Jeong-Seop Singer, Joshua H. Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title | Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title_full | Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title_fullStr | Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title_full_unstemmed | Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title_short | Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses |
title_sort | complexin 3 increases the fidelity of signaling in a retinal circuit by regulating exocytosis at ribbon synapses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5134263/ https://www.ncbi.nlm.nih.gov/pubmed/27239031 http://dx.doi.org/10.1016/j.celrep.2016.05.012 |
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