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.
Photoreceptor proteins typically consist of a protein attached to a non-protein chromophore (sometimes referred as photopigment, even so photopigment may also refer to the photoreceptor as a whole). The chromophore reacts to light via photoisomerization or photoreduction, thus initiating a change of the receptor protein which triggers a signal transduction cascade. Chromophores found in photoreceptors include retinal (retinylidene proteins, for example rhodopsin in animals), flavin (flavoproteins, for example cryptochrome in plants and animals) and bilin (biliproteins, for example phytochrome in plants). The plant protein UVR8 is exceptional amongst photoreceptors in that it contains no external chromophore. Instead, UVR8 absorbs light through tryptophan residues within its protein coding sequence.
Photoreceptor cell
Melanopsin: in vertebrate retina, mediates pupillary reflex, involved in regulation of circadian rhythms
Photopsin: reception of various colors of light in the cone cells of vertebrate retina
Rhodopsin: green-blue light reception in the rod cells of vertebrate retina
Protein Kinase C: mediates photoreceptor deactivation, and retinal degeneration
OPN5: sensitive to UV-light
UVR8: UV-B light reception
Cryptochrome: blue and UV-A light reception
Phototropin: blue and UV-A light perception (to mediate phototropism and chloroplast movement)
Zeitlupe: blue light entrainment of the circadian clock
Phytochrome: red and far-red light reception
All the photoreceptors listed above allow plants to sense light with wavelengths range from 280 nm (UV-B) to 750 nm (far-red light).
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Photopigments are unstable pigments that undergo a chemical change when they absorb light. The term is generally applied to the non-protein chromophore moiety of photosensitive chromoproteins, such as the pigments involved in photosynthesis and photoreception. In medical terminology, "photopigment" commonly refers to the photoreceptor proteins of the retina. Photosynthetic pigment Photosynthetic pigments convert light into biochemical energy. Examples for photosynthetic pigments are chlorophyll, carotenoids and phycobilins.
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.
Visual phototransduction is the sensory transduction process of the visual system by which light is detected to yield nerve impulses in the rod cells and cone cells in the retina of the eye in humans and other vertebrates. It relies on the visual cycle, a sequence of biochemical reactions in which a molecule of retinal bound to opsin undergoes photoisomerization, initiates a cascade that signals detection of the photon, and is indirectly restored to its photosensitive isomer for reuse.
Explores the electromagnetic spectrum, optical sensors, human retina, color synthesis, light polarization, photon-material interaction, and X-ray interactions.
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The plant ultraviolet-B (UV-B) photoreceptor UVR8 plays an important role in UV-B acclimation and survival. UV-B absorption by homodimeric UVR8 induces its monomerization and interaction with the E3 ubiquitin ligase COP1, leading ultimately to gene express ...
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Information about a moving object is usually poor at each retinotopic location because photoreceptor activation is short, noisy, and affected by shadows, reflections of other objects, and so on. Integration across the motion trajectory may yield a much bet ...