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Analyzing the Complexins of the photoreceptor ribbon synapses in mouse retina

Subject Area Molecular Biology and Physiology of Neurons and Glial Cells
Term from 2019 to 2022
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 428863786
 
Final Report Year 2023

Final Report Abstract

In our study, we set out to examine the function of the Complexins (Cplxs) 3 and 4 in photoreceptor ribbon synapses of mouse retina. The key findings of our study are: Cplx3 expression is not regulated by light but by the circadian rhythm. - Cplx4 expression changes light-dependently at the protein but not the transcript level. - Soluble and membrane-associated Cplx3 and Cplx4 pools exist simultaneously in the mouse retina. Their subcellular distribution – soluble versus membrane-associated – does not change light-dependently. - Cplx3 and Cplx4 most likely interact with SVs in a farnesylation-dependent manner. - The Cplx4-SNARE complex interacts with the G-protein Transducin in vitro. - Hypothesis: Transducin, which is known to translocate light-dependently from the outer segment to the synaptic terminal of rod photoreceptors, signals the state of rod photoreceptor adaptation to their ribbon synapse via a putative interaction with the Cplx4- SNARE complex. This interaction throttles the light-dependent replenishment of readily releasable SVs and sustained SV exocytosis.

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