Abstract
The cone synapse is a complex signaling hub composed of the cone photoreceptor terminal and the dendrites of bipolar and horizontal cells converging around multiple ribbon synapses. Factors that promote organization of this structure are largely unexplored. In this study we characterize the localization of adhesion and scaffolding proteins that are localized to the cone synapse, including alpha-n-catenin, beta-catenin, gamma-protocadherin, cadherin-8, MAGI2 and CASK. We describe the localization of these proteins during development of the mouse retina and in the adult macaque retina and find that these proteins are concentrated at the cone synapse. The localization of these proteins was then characterized at the cellular and subcellular levels. Alpha-n-catenin, gamma-protocadherin and cadherin-8 were concentrated in the dendrites of bipolar cells that project to the cone synapse but were not detected or stained very dimly in the dendrites of cells projecting to rod synapses. This study adds to our knowledge of cone synapse development by characterizing the developmental localization of these factors and identifies these factors as candidates for functional analysis of cone synapse formation.