Channelrhodopsins are a subfamily of retinylidene proteins (rhodopsins) that function as light-gated ion channels. They serve as sensory photoreceptors in unicellular green algae, controlling phototaxis: movement in response to light. Expressed in cells of other organisms, they enable light to control electrical excitability, intracellular acidity, calcium influx, and other cellular processes (see optogenetics). Channelrhodopsin-1 (ChR1) and Channelrhodopsin-2 (ChR2) from the model organism Chlamydomonas reinhardtii are the first discovered channelrhodopsins. Variants that are sensitive to different colors of light or selective for specific ions (ACRs, KCRs) have been cloned from other species of algae and protists. Phototaxis and photoorientation of microalgae have been studied over more than hundred years in many laboratories worldwide. In 1980, Ken Foster developed the first consistent theory about the functionality of algal eyes. He also analyzed published action spectra and complemented blind cells with retinal and retinal analogues, which led to the conclusion that the photoreceptor for motility responses in Chlorophyceae is rhodopsin. Photocurrents of the Chlorophyceae Heamatococcus pluvialis and Chlamydomonas reinhardtii were studied over many years in the groups of Oleg Sineshchekov and Peter Hegemann. Based on action spectroscopy and simultaneous recordings of photocurrents and flagellar beating, it was determined that the photoreceptor currents and subsequent flagellar movements are mediated by rhodopsin and control phototaxis and photophobic responses. The extremely fast rise of the photoreceptor current after a brief light flash led to the conclusion that the rhodopsin and the channel are intimately linked in a protein complex, or even within one single protein. The name "channelrhodopsin" was coined to highlight this unusual property, and the sequences were renamed accordingly. The nucleotide sequences of the rhodopsins now called channelrhodopsins ChR1 and ChR2 were finally uncovered in a large-scale EST sequencing project in C.

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Concepts associés (3)
Photoreceptor protein
Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals.
Optogénétique
L'optogénétique est un domaine de recherche et d’application associant les techniques de l’optique à celles de la génétique. Elle permet, par une stimulation lumineuse, d'altérer spécifiquement et localement un nombre limité de cellules modifiées génétiquement pour y être sensibles, sans perturber directement l'état des cellules voisines. Conceptualisée à la fin des années 1970, elle est consacrée par un mot dédié en 2006, puis élue méthode de l’année par Nature Methods en 2010.
Rhodopsine
La rhodopsine (du grec ῥόδος rhodos, rose, et ὄψομαι opsomai, futur du verbe ὁρῶ orô, voir) ou pourpre rétinien est un pigment protéique photosensible présent dans les bâtonnets, l'un des deux types des cellules photoréceptrices de la rétine (œil des vertébrés, œil composé des arthropodes, ocelles). C'est également un récepteur couplé aux protéines G. Elle est responsable de la sensibilité de l'œil à la lumière. Comme tous les récepteurs couplés aux protéines G, la rhodopsine possède 7 domaines transmembranaires.
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Cellular Mechanisms of Brain Function
This course aims for a mechanistic description of mammalian brain function at the level of individual nerve cells and their synaptic interactions.
Cellular Mechanisms of Brain Function
This course aims for a mechanistic description of mammalian brain function at the level of individual nerve cells and their synaptic interactions.