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 t...
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2016-06-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124716305794 |
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doaj-3c96857817d840289321a4eb859042102020-11-24T21:47:23ZengElsevierCell Reports2211-12472016-06-0115102239225010.1016/j.celrep.2016.05.012Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon SynapsesLena S. Mortensen0Silvia J.H. Park1Jiang-bin Ke2Benjamin H. Cooper3Lei Zhang4Cordelia Imig5Siegrid Löwel6Kerstin Reim7Nils Brose8Jonathan B. Demb9Jeong-Seop Rhee10Joshua H. Singer11Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Ophthalmology and Visual Science, Yale University, New Haven, CT 06511, USADepartment of Biology, University of Maryland, College Park, MD 20742, USADepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Biology, University of Maryland, College Park, MD 20742, USADepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Systems Neuroscience, Bernstein Focus Neurotechnology, Johann-Friedrich-Blumenbach Institute for Zoology and Anthropology, University of Göttingen, 37075 Göttingen, GermanyDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Ophthalmology and Visual Science, Yale University, New Haven, CT 06511, USADepartment of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, 37075 Göttingen, GermanyDepartment of Biology, University of Maryland, College Park, MD 20742, USAComplexin (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 Ca2+-dependent transmission, dependent on local [Ca2+] nanodomains, but enhanced slower Ca2+-dependent transmission, dependent on global intraterminal [Ca2+] ([Ca2+]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.http://www.sciencedirect.com/science/article/pii/S2211124716305794 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Lena S. Mortensen Silvia J.H. Park Jiang-bin Ke Benjamin H. Cooper Lei Zhang Cordelia Imig Siegrid Löwel Kerstin Reim Nils Brose Jonathan B. Demb Jeong-Seop Rhee Joshua H. Singer |
| spellingShingle |
Lena S. Mortensen Silvia J.H. Park Jiang-bin Ke Benjamin H. Cooper Lei Zhang Cordelia Imig Siegrid Löwel Kerstin Reim Nils Brose Jonathan B. Demb Jeong-Seop Rhee Joshua H. Singer Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses Cell Reports |
| author_facet |
Lena S. Mortensen Silvia J.H. Park Jiang-bin Ke Benjamin H. Cooper Lei Zhang Cordelia Imig Siegrid Löwel Kerstin Reim Nils Brose Jonathan B. Demb Jeong-Seop Rhee Joshua H. Singer |
| author_sort |
Lena S. Mortensen |
| title |
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_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_sort |
complexin 3 increases the fidelity of signaling in a retinal circuit by regulating exocytosis at ribbon synapses |
| publisher |
Elsevier |
| series |
Cell Reports |
| issn |
2211-1247 |
| publishDate |
2016-06-01 |
| 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 Ca2+-dependent transmission, dependent on local [Ca2+] nanodomains, but enhanced slower Ca2+-dependent transmission, dependent on global intraterminal [Ca2+] ([Ca2+]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. |
| url |
http://www.sciencedirect.com/science/article/pii/S2211124716305794 |
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