title: The molecular basis of mechanisms underlying polarization vision.
abstract: The underlying mechanisms of polarization sensitivity (PS) have long remained elusive. For rhabdomeric photoreceptors, questions remain over the high levels of PS measured experimentally. In ciliary photoreceptors, and specifically cones, little direct evidence supports any type of mechanism. In order to promote a greater interest in these fundamental aspects of polarization vision, we examined a varied collection of studies linking membrane biochemistry, protein-protein interactions, molecular ordering and membrane phase behaviour. While initially these studies may seem unrelated to polarization vision, a common narrative emerges. A surprising amount of evidence exists demonstrating the importance of protein-protein interactions in both rhabdomeric and ciliary photoreceptors, indicating the possible long-range ordering of the opsin protein for increased PS. Moreover, we extend this direction by considering how such protein paracrystalline organization arises in all cell types from controlled membrane phase behaviour and propose a universal pathway for PS to occur in both rhabdomeric and cone photoreceptors.
authors.affiliation: School of Biological Sciences, University of Bristol, Woodland Road, Bristol BS8 1UG, UK. nicholas.roberts@bristol.ac.uk
authors.forename: Nicholas W
authors.initials: NW
authors.lastname: Roberts
authors.forename: Megan L
authors.initials: ML
authors.lastname: Porter
authors.forename: Thomas W
authors.initials: TW
authors.lastname: Cronin
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D008027:Light; D055355:Opsins / Q000502:physiology; D010786:Photoreceptor Cells / Q000502:physiology*; D017949:Retinal Cone Photoreceptor Cells / Q000502:physiology*; D014785:Vision, Ocular / Q000502:physiology*
chemical_list: D055355:Opsins