Looking within for Vision

Abstract

(Neuron 50, 1–3; April 6, 2006) The authors wish to correct three errors in the preview relating to the chromophore used by Channelrhodopsin-2. The first sentence should read: “Channelrhodopsin-2 (ChR2), a directly light-gated cation channel from the green alga Chlamydomonas reinhardtii, has been shown to be a directly light-switched cation-selective ion channel, which employs all-trans retinal as its chromophore (Nagel, 2005).” In the fifth paragraph, the second sentence should read: “The channelopsin-2 (Chop2) protein, originally discovered in green algae, utilizes the light-sensitive chromophore—all-trans retinal—whereas the rod photoreceptor photopigment rhodopsin uses 11-cis retinal.” In Figure 1, the retinal chromophore for channelrhodopsin was misdrawn in the diagram. In the dark, the chromophore is all-trans retinal, and light isomerizes this to the 11-cis configuration. The corrected figure is printed here. Looking within for VisionFlannery et al.NeuronApril 06, 2006In BriefChannelrhodopsin-2 (ChR2), a directly light-gated cation channel from the green alga Chlamydomonas reinhardtii has been shown to be a directly light-switched cation-selective ion channel, which employs 11-cis retinal as its chromophore. This is the same chromophore as the mammalian photoreceptor's visual pigment—rhodopsin. Previously, investigators demonstrated that ChR2 can be used to optically control neuronal firing by depolarizing the cell. In this issue of Neuron, Bi et al. apply viral-mediated gene transfer to deliver ChR2 to retinal ganglion cells (RGC) in a rodent model of inherited blindness. Full-Text PDF Open Archive