When a photon is absorbed, 11-cis-retinal is transformed to all-trans-retinal, and it moves to the exit site of rhodopsin. It will not leave the opsin protein until another fresh chromophore comes to replace it, except for in the ABCR pathway. Whilst still bound to the opsin, all-trans-retinal is transformed into all-trans-retinol by all-trans-Retinol Dehydrogenase. It then proceeds to the cell membrane of the rod, where it is chaperoned to the Retinal Pigment Epithelium (RPE) by Interphotoreceptor retinoid-binding protein (IRBP). It then enters the RPE cells, and is transferred to the Cellular Retinol Binding Protein (CRBP) chaperone.
When inside the RPE cell, bound to CRBP, the all-trans-retinol is esterified by Lecithin Retinol Acyltransferase (LRAT) to form a retinyl ester. The retinyl esters of the RPE are chaperoned by a protein known as RPE65. It is in this form that the RPE stores most of its retinoids, as the RPE stores 2-3 times more retinoids than the neural retina itself. When further chromophore is required, the retinyl esters are acted on by isomerohydrolase to produce 11-cis-retinol, which is transferred to the Cellular retinaldehyde binding protein (CRALBP). 11-cis-Retinol is transformed into 11-cis retinal by 11-cis-retinol dehydrogenase, then it is shipped back to the photoreceptor cells via IRBP. There, it replaces the spent chromophore in opsin molecules, rendering the opsin photosensitive.