Forskning ved Københavns Universitet - Københavns Universitet


Complexin 3 Increases the Fidelity of Signaling in a Retinal Circuit by Regulating Exocytosis at Ribbon Synapses

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  • Lena S Mortensen
  • Silvia J H Park
  • Jiang-Bin Ke
  • Benjamin H Cooper
  • Lei Zhang
  • Imig, Cordelia
  • Siegrid Löwel
  • Kerstin Reim
  • Nils Brose
  • Jonathan B Demb
  • Jeong-Seop Rhee
  • Joshua H Singer

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.

TidsskriftCell Reports
Udgave nummer10
Sider (fra-til)2239-2250
Antal sider12
StatusUdgivet - 7 jun. 2016
Eksternt udgivetJa

ID: 237697975