| Home > Publications Database > Higher-order architecture of rhodopsin in intact photoreceptors and its implication for phototransduction kinetics. |
| Journal Article | DZNE-2020-04197 |
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2015
Cell Press
Cambridge, Mass.
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Please use a persistent id in citations: doi:10.1016/j.str.2015.01.015
Abstract: The visual pigment rhodopsin belongs to the family of G protein-coupled receptors that can form higher oligomers. It is controversial whether rhodopsin forms oligomers and whether oligomers are functionally relevant. Here, we study rhodopsin organization in cryosections of dark-adapted mouse rod photoreceptors by cryoelectron tomography. We identify four hierarchical levels of organization. Rhodopsin forms dimers; at least ten dimers form a row. Rows form pairs (tracks) that are aligned parallel to the disk incisures. Particle-based simulation shows that the combination of tracks with fast precomplex formation, i.e. rapid association and dissociation between inactive rhodopsin and the G protein transducin, leads to kinetic trapping: rhodopsin first activates transducin from its own track, whereas recruitment of transducin from other tracks proceeds more slowly. The trap mechanism could produce uniform single-photon responses independent of rhodopsin lifetime. In general, tracks might provide a platform that coordinates the spatiotemporal interaction of signaling molecules.
Keyword(s): Animals (MeSH) ; Kinetics (MeSH) ; Mice (MeSH) ; Mice, Inbred C57BL (MeSH) ; Photoreceptor Cells: metabolism (MeSH) ; Photoreceptor Cells: ultrastructure (MeSH) ; Protein Binding (MeSH) ; Protein Multimerization (MeSH) ; Rhodopsin: chemistry (MeSH) ; Rhodopsin: metabolism (MeSH) ; Transducin: metabolism (MeSH) ; Vision, Ocular (MeSH) ; Rhodopsin ; Transducin
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