Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering
The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived fr...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-06-01
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| Series: | Frontiers in Chemistry |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fchem.2022.879609/full |
| _version_ | 1811241576823783424 |
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| author | Willem J. de Grip Willem J. de Grip Srividya Ganapathy |
| author_facet | Willem J. de Grip Willem J. de Grip Srividya Ganapathy |
| author_sort | Willem J. de Grip |
| collection | DOAJ |
| description | The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential. |
| first_indexed | 2024-04-12T13:38:14Z |
| format | Article |
| id | doaj.art-56817ff8ba4b4a0797fe6fe67d58640a |
| institution | Directory Open Access Journal |
| issn | 2296-2646 |
| language | English |
| last_indexed | 2024-04-12T13:38:14Z |
| publishDate | 2022-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj.art-56817ff8ba4b4a0797fe6fe67d58640a2022-12-22T03:30:56ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462022-06-011010.3389/fchem.2022.879609879609Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative EngineeringWillem J. de Grip0Willem J. de Grip1Srividya Ganapathy2Leiden Institute of Chemistry, Department of Biophysical Organic Chemistry, Leiden University, Leiden, NetherlandsRadboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, NetherlandsDepartment of Imaging Physics, Delft University of Technology, NetherlandsThe first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential.https://www.frontiersin.org/articles/10.3389/fchem.2022.879609/fullmembrane proteinphotoreceptorretinal proteinvisual pigmentsoptogeneticsion pumps |
| spellingShingle | Willem J. de Grip Willem J. de Grip Srividya Ganapathy Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering Frontiers in Chemistry membrane protein photoreceptor retinal protein visual pigments optogenetics ion pumps |
| title | Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering |
| title_full | Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering |
| title_fullStr | Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering |
| title_full_unstemmed | Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering |
| title_short | Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering |
| title_sort | rhodopsins an excitingly versatile protein species for research development and creative engineering |
| topic | membrane protein photoreceptor retinal protein visual pigments optogenetics ion pumps |
| url | https://www.frontiersin.org/articles/10.3389/fchem.2022.879609/full |
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