Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses
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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.
In: Cell Reports, Vol. 15, No. 10, 07.06.2016, p. 2239-2250.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses
AU - Mortensen, Lena S
AU - Park, Silvia J H
AU - Ke, Jiang-Bin
AU - Cooper, Benjamin H
AU - Zhang, Lei
AU - Imig, Cordelia
AU - Löwel, Siegrid
AU - Reim, Kerstin
AU - Brose, Nils
AU - Demb, Jonathan B
AU - Rhee, Jeong-Seop
AU - Singer, Joshua H
N1 - Copyright © 2016 The Author(s). Published by Elsevier Inc. All rights reserved.
PY - 2016/6/7
Y1 - 2016/6/7
N2 - 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.
AB - 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.
KW - Animals
KW - Calcium/pharmacology
KW - Exocytosis/drug effects
KW - Eye Proteins/metabolism
KW - Mice, Inbred C57BL
KW - Multivesicular Bodies/drug effects
KW - Nerve Tissue Proteins/deficiency
KW - Retina/cytology
KW - Retinal Bipolar Cells/drug effects
KW - Signal Transduction/drug effects
KW - Synapses/drug effects
KW - Synaptic Transmission/drug effects
U2 - 10.1016/j.celrep.2016.05.012
DO - 10.1016/j.celrep.2016.05.012
M3 - Journal article
C2 - 27239031
VL - 15
SP - 2239
EP - 2250
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 10
ER -
ID: 237697975